Targeting Tumor Dormancy and Recurrence: Molecular Mechanisms and Peptide Therapeutic Delivery

Abstract

Tumor dormancy is a clinically challenging but physiologically significant aspect of cancer development, characterized by disseminated tumor cells that persist in non-proliferative, quiescent state and frequently serving as a risk factor of recurrence. Although extensive progress has been made in understanding cancer progression and metastasis, strategies for reliably detecting and eliminating dormant tumor cells remain limited. This review aims to evaluate the current understanding of the molecular mechanisms underlying tumor dormancy, cellular quiscence, angiogenic processes, immune surveillance, and the complex roles of the tumor microenvironment, including extracellular matrix remodeling, metabolic adaptation and niche protection in tumor dormancy. Particular attention is given to the challenges associated with detecting and eliminating dormant cells, because these cells exhibit resistance to conventional therapies and reveal evasion of immune responses. Furthermore, we highlight peptide-based strategies as promising platforms for detection, modulation and elimination of dormant tumor cells. These include tumor-penetrating peptides, peptide-drug conjugates, self-assembling peptide nanostructures, and hydrogel–based delivery systems designed to disrupt dormancy-maintaining niches or sensitize dormant cells to therapeutic intervention. The review also provides a summary of recent preclinical and clinical developments in peptide-based treatments and outlines approaches to overcome translational challenges in targeting tumor dormancy. By integrating advances in peptide engineering with the biological principles of tumor dormancy, this review underscores the potential of peptide-based platforms to improve therapeutic outcomes and reduce cancer recurrence.

References

[1] F. Bray, M. Laversanne, H. Sung, et al., “Global Cancer Statistics 2022: GLOBOCAN Estimates of Incidence and Mortality Worldwide for 36 Cancers in 185 Countries,” CA: A Cancer Journal for Clinicians74, no. 3 (2024): 229–263.

[2] L. Schmallenbach, M. Bley, T. W. Bärnighausen, C. R. Sugimoto, C. Lerchenmüller, and M. J. Lerchenmueller, “Global Distribution of Research Efforts, Disease Burden, and Impact of US Public Funding Withdrawal,” Nature Medicine31 (2025): 3101–3109.

[3] A. Soragni, E. S. Knudsen, T. N. O'Connor, et al., “Acquired Resistance in Cancer: Towards Targeted Therapeutic Strategies,” Nature Reviews Cancer25 (2025): 613–633.

[4] M. Ge, X.-Y. Chen, P. Huang, et al., “Understanding and Overcoming Multidrug Resistance in Cancer,” Nature Reviews Clinical Oncology22 (2025): 760–780.

[5] Y. Gu, R. Yang, Y. Zhang, et al., “Molecular Mechanisms and Therapeutic Strategies in Overcoming Chemotherapy Resistance in Cancer,” Molecular Biomedicine6, no. 1 (2025): 2.

[6] E. T. Goddard, M. H. Linde, S. Srivastava, et al., “Immune Evasion of dormant Disseminated Tumor Cells Is Due to Their Scarcity and can be Overcome by T Cell Immunotherapies,” Cancer Cell42, no. 1 (2024): 119–134.e12.

[7] J. Agudo, J. A. Aguirre-Ghiso, M. Bhatia, L. A. Chodosh, A. L. Correia, and C. A. Klein, “Targeting Cancer Cell Dormancy,” Nature Reviews Cancer24, no. 2 (2024): 97–104.

[8] K. Zhao, T. Sun, Q. Sun, et al., “Nerve Growth Factor Signaling Promotes Nuclear Translocation of TRAF4 to Enhance Tumor Stemness and Metastatic Dormancy via C-Jun-Mediated IL-8 Autocrine,” Advanced Science12, no. 7 (2025): 2414437.

[9] A. Brooks, Y. Zhang, J. Chen, and C. X. Zhao, “Cancer Metastasis-On-A-Chip for Modeling Metastatic Cascade and Drug Screening,” Advanced Healthcare Materials13, no. 21 (2024): 2302436.

[10] F. Xu, Y. Liu, Z. Que, et al., “Recent Advancements in Lung Cancer Metastasis Prevention Based on Nanostrategies,” Advanced Science12, no. 23 (2025): 2409293.

[11] L. Qiao, G. Zhu, T. Jiang, et al., “Self-Destructive Copper Carriers Induce Pyroptosis and Cuproptosis for Efficient Tumor Immunotherapy Against Dormant and Recurrent Tumors,” Advanced Materials36, no. 8 (2024): 2308241.

[12] E. Risson, A. R. Nobre, V. Maguer-Satta, and J. A. Aguirre-Ghiso, “The Current Paradigm and Challenges Ahead for the Dormancy of Disseminated Tumor Cells,” Nature Cancer1, no. 7 (2020): 672–680.

[13] C. J. Farino Reyes, S. Pradhan, and J. H. Slater, “The Influence of Ligand Density and Degradability on Hydrogel Induced Breast Cancer Dormancy and Reactivation,” Advanced Healthcare Materials10, no. 11 (2021): 2002227.

[14] Ö. Şen, M. Emanet, and G. Ciofani, “Nanotechnology-Based Strategies to Evaluate and Counteract Cancer Metastasis and Neoangiogenesis,” Advanced Healthcare Materials10, no. 10 (2021): 2002163.

[15] C. J. Farino, S. Pradhan, and J. H. Slater, “The Influence of Matrix-Induced Dormancy on Metastatic Breast Cancer Chemoresistance,” ACS Applied Bio Materials3, no. 9 (2020): 5832–5844.

[16] G. Xia, H. Zhang, R. Cheng, et al., “Localized Controlled Delivery of Gemcitabine via Microsol Electrospun Fibers to Prevent Pancreatic Cancer Recurrence,” Advanced Healthcare Materials7, no. 18 (2018): 1800593.

[17] K. S. Abdelwahed, A. B. Siddique, M. H. Qusa, et al., “PCSK9 Axis-Targeting Pseurotin a as a Novel Prostate Cancer Recurrence Suppressor Lead,” ACS Pharmacology & Translational Science4, no. 6 (2021): 1771–1781.

[18] Q. Liu, F. Chen, L. Hou, et al., “Nanocarrier-Mediated Chemo-Immunotherapy Arrested Cancer Progression and Induced Tumor Dormancy in Desmoplastic Melanoma,” ACS Nano12, no. 8 (2018): 7812–7825.

[19] G. Tiram, E. Segal, A. Krivitsky, et al., “Identification of Dormancy-Associated Micrornas for the Design of Osteosarcoma-Targeted Dendritic Polyglycerol Nanopolyplexes,” ACS Nano10 (2016): 2028e2045.

[20] Y. Fang, Z. Liu, H. Wang, et al., “Implantable Sandwich-Like Scaffold/Fiber Composite Spatiotemporally Releasing Combretastatin A4 and Doxorubicin for Efficient Inhibition of Postoperative Tumor Recurrence,” ACS Applied Materials & Interfaces14, no. 24 (2022): 27525–27537.

[21] O. M. Rueda, S.-J. Sammut, J. A. Seoane, et al., “Dynamics of Breast-Cancer Relapse Reveal Late-Recurring ER-Positive Genomic Subgroups,” Nature567, no. 7748 (2019): 399–404.

[22] C. Song, X. Wu, J. Wang, R. Liu, and Y. Zhao, “Photosensitizer-Immunotherapy Integrated Microneedles for Preventing Tumor Recurrence and Metastasis,” Nano Today51 (2023): 101913.

[23] J. Zhang, Y. Guo, G. Pan, et al., “Injectable Drug-Conjugated DNA Hydrogel for Local Chemotherapy to Prevent Tumor Recurrence,” ACS Applied Materials & Interfaces12, no. 19 (2020): 21441–21449.

[24] J. A. Aguirre-Ghiso, “Models, Mechanisms and Clinical Evidence for Cancer Dormancy,” Nature Reviews Cancer7, no. 11 (2007): 834–846.

[25] S. Yang, J. Seo, J. Choi, et al., “Towards Understanding Cancer Dormancy Over Strategic Hitching up Mechanisms to Technologies,” Molecular Cancer24 (2025): 47.

[26] Y. Suhail, M. P. Cain, K. Vanaja, et al., “Systems Biology of Cancer Metastasis,” Cell Systems9, no. 2 (2019): 109–127.

[27] A. Dasgupta, A. R. Lim, and C. M. Ghajar, “Circulating and Disseminated Tumor Cells: Harbingers or Initiators of Metastasis,” Molecular Oncology11, no. 1 (2017): 40–61.

[28] S. Qin, B. Li, H. Ming, E. C. Nice, B. Zou, and C. Huang, “Harnessing Redox Signaling to Overcome Therapeutic-Resistant Cancer Dormancy,” Biochimica et Biophysica Acta (BBA)—Reviews on Cancer1877, no. 4 (2022): 188749.

[29] O. Hen and D. Barkan, “Dormant Disseminated Tumor Cells and Cancer Stem/Progenitor-Like Cells: Similarities and Opportunities,” Seminars in Cancer Biology60 (2020): 157–165.

[30] K. Santos-de-Frutos and N. Djouder, “When Dormancy Fuels Tumour Relapse,” Communications Biology4, no. 1 (2021): 747.

[31] S. Bhattacharya, A. Mohanty, S. Achuthan, et al., “Group Behavior and Emergence of Cancer Drug Resistance,” Trends in Cancer7, no. 4 (2021): 323–334.

[32] S. Bakhshandeh, U. Heras, H. M. Taïeb, et al., “Dormancy-Inducing 3D Engineered Matrix Uncovers Mechanosensitive and Drug-Protective FHL2-p21 Signaling Axis,” Science Advances10, no. 45 (2024): eadr3997.

[33] C. A. Klein, “Cancer Progression and the Invisible Phase of Metastatic Colonization,” Nature Reviews Cancer20, no. 11 (2020): 681–694.

[34] S. S. Rao, R. V. Kondapaneni, and A. A. Narkhede, “Bioengineered Models to Study Tumor Dormancy,” Journal of Biological Engineering13, no. 1 (2019): 3.

[35] H. Kim, A. Wirasaputra, F. Mohammadi, et al., “Live Cell Lineage Tracing of Dormant Cancer Cells,” Advanced Healthcare Materials12, no. 14 (2023): 2202275.

[36] S. Galarza, A. J. Crosby, C. Pak, and S. R. Peyton, “Control of Astrocyte Quiescence and Activation in a Synthetic Brain Hydrogel,” Advanced Healthcare Materials9, no. 4 (2020): e1901419.

[37] K. Goodarzi, P. Sarker, and S. S. Rao, “Regulation of Brain Metastatic Breast Cancer Cell Dormancy Versus Proliferation on Hyaluronic Acid Hydrogels via Laminin and Laminin-Derived Peptides,” ACS Applied Bio Materials8, no. 4 (2025): 2824–2837.

[38] J. Y. Fang, S.-J. Tan, Y.-C. Wu, Z. Yang, B. X. Hoang, and B. Han, “From Competency to Dormancy: A 3D Model to Study Cancer Cells and Drug Responsiveness,” Journal of Translational Medicine14 (2016): 38.

[39] S. K. Schmidt, S. Fischer, Z. El Ahmad, et al., “Modeling a Mesenchymal Cell State by Bioprinting for the Molecular Analysis of Dormancy in Melanoma,” Materials Today Bio32 (2025): 101674.

[40] A. R. Aleem, L. Shahzadi, F. Alvi, et al., “Thyroxin Releasing Chitosan/Collagen Based Smart Hydrogels to Stimulate Neovascularization,” Materials & Design133 (2017): 416–425.

[41] A. R. Aleem, L. Shahzadi, M. Nasir, et al., “Developing Sulfur-Doped Titanium Oxide Nanoparticles Loaded Chitosan/Cellulose-Based Proangiogenic Dressings for Chronic Ulcer and Burn Wounds Healing,” Journal of Biomedical Materials Research, Part B: Applied Biomaterials110, no. 5 (2022): 1069–1081.

[42] A. R. Aleem, L. Shahzadi, S. Tehseen, et al., “Amino Acids Loaded Chitosan/Collagen Based New Membranes Stimulate Angiogenesis in Chorioallantoic Membrane Assay,” International Journal of Biological Macromolecules140 (2019): 401–406.

[43] A. R. Aleem, J. Liu, J. Wang, et al., “Selective Sensing of Cu²⁺ and Fe³⁺ Ions With Vis-Excitation Using Fluorescent Eu³⁺-Induced Aggregates of Polysaccharides (EIAP) in Mammalian Cells and Aqueous Systems,” Journal of Hazardous Materials399 (2020): 122991.

[44] A. R. Aleem, W. Ding, J. Liu, et al., “Visible-Light Excitable Eu³⁺-Induced Hyaluronic Acid-Chitosan Aggregates With Heterocyclic Ligands for Sensitive and Fast Recognition of Hazardous Ions,” International Journal of Biological Macromolecules184 (2021): 188–199.

[45] A. R. Aleem, R. Chen, T. Wan, et al., “Highly Water-Soluble and Biocompatible Hyaluronic Acid Functionalized Upconversion Nanoparticles as Ratiometric Nanoprobes for Label-Free Detection of Nitrofuran and Doxorubicin,” Food Chemistry438 (2023): 137961.

[46] D. G. Leach, S. Young, and J. D. Hartgerink, “Advances in Immunotherapy Delivery From Implantable and Injectable Biomaterials,” Acta Biomaterialia88 (2019): 15–31.

[47] Y. Qi, H. Min, A. Mujeeb, et al., “Injectable Hexapeptide Hydrogel for Localized Chemotherapy Prevents Breast Cancer Recurrence,” ACS Applied Materials & Interfaces10, no. 8 (2018): 6972–6981.

[48] R. Chang, Q. Zou, R. Xing, and X. Yan, “Peptide-Based Supramolecular Nanodrugs as a New Generation of Therapeutic Toolboxes Against Cancer,” Advanced Therapeutics2, no. 8 (2019): 1900048.

[49] D. Kim, J. W. Lee, P. A. Rawding, et al., “Dendrimer Conjugates With PD-L1-Binding Peptides Enhance In Vivo Antitumor Immune Response,” Advanced Healthcare Materials14, no. 20 (2025): 2500551.

[50] Z. Wang, H. Luo, H. Wang, et al., “Peptide-Based Supramolecular Therapeutics for Fighting Major Diseases,” Advanced Functional Materials34, no. 25 (2024): 2314492.

[51] X. Luan, H. Kong, P. He, et al., “Self-Assembled Peptide-Based Nanodrugs: Molecular Design, Synthesis, Functionalization, and Targeted Tumor Bioimaging and Biotherapy,” Small19, no. 3 (2023): 2205787.

[52] H. Hong, Q. Zou, Y. Liu, S. Wang, G. Shen, and X. Yan, “Supramolecular Nanodrugs Based on Covalent Assembly of Therapeutic Peptides Toward In Vitro Synergistic Anticancer Therapy,” ChemMedChem16, no. 15 (2021): 2381–2385.

[53] Y. Huo, J. Hu, Y. Yin, P. Liu, K. Cai, and W. Ji, “Self-Assembling Peptide-Based Functional Biomaterials,” ChemBioChem24, no. 2 (2023): e202200582.

[54] T. G. Phan and P. I. Croucher, “The Dormant Cancer Cell Life Cycle,” Nature Reviews Cancer20, no. 7 (2020): 398–411.

[55] W. A. Weston and A. R. Barr, “A Cell Cycle Centric View of Tumour Dormancy,” British Journal of Cancer129, no. 10 (2023): 1535–1545.

[56] L. Lanzetti, “Oncometabolites at the Crossroads of Genetic, Epigenetic and Ecological Alterations in Cancer,” Cell Death & Differentiation31 (2024): 1582–1594.

[57] M. El-Tanani, S. A. Rabbani, R. Babiker, et al., “Unraveling the Tumor Microenvironment: Insights Into Cancer Metastasis and Therapeutic Strategies,” Cancer Letters591 (2024): 216894.

[58] T. Liu, C. Lu, X. Jiang, et al., “Nano-Based Strategies Aiming at Tumor Microenvironment for Improved Cancer Therapy,” Molecular Pharmaceutics22, no. 2 (2025): 647–677.

[59] S. Flores-Torres, T. Jiang, J. Kort-Mascort, et al., “Constructing 3D In Vitro Models of Heterocellular Solid Tumors and Stromal Tissues Using Extrusion-Based Bioprinting,” ACS Biomaterials Science & Engineering9, no. 2 (2023): 542–561.

[60] H. Endo and M. Inoue, “Dormancy in Cancer,” Cancer Science110, no. 2 (2019): 474–480.

[61] M. P. F. Damen, J. van Rheenen, and C. L. G. J. Scheele, “Targeting Dormant Tumor Cells to Prevent Cancer Recurrence,” FEBS journal288, no. 21 (2021): 6286–6303.

[62] O. G. Dobbs and D. Coverley, Chromatin Dynamics During Entry to Quiescence and Compromised Functionality in Cancer Cells. Nuclear, Chromosomal, and Genomic Architecture in Biology and Medicine (Springer, 2022), 279–294.

[63] M. M. Afifi, A. Crncec, J. A. Cornwell, et al., “Irreversible Cell Cycle Exit Associated With Senescence Is Mediated by Constitutive MYC Degradation,” Cell Reports42, no. 9 (2023): 113079.

[64] O. Marescal and I. M. Cheeseman, “Cellular Mechanisms and Regulation of Quiescence,” Developmental Cell55, no. 3 (2020): 259–271.

[65] X. Shi, H. Zhang, H. Paddon, G. Lee, X. Cao, and S. Pelech, “Phosphorylation of STAT3 Serine-727 by Cyclin-Dependent Kinase 1 Is Critical for Nocodazole-Induced Mitotic Arrest,” Biochemistry45, no. 18 (2006): 5857–5867.

[66] H. Xiao, J. Wang, L. Yuan, C. Xiao, Y. Wang, and X. Liu, “Chicoric Acid Induces Apoptosis in 3T3-L1 Preadipocytes Through ROS-Mediated PI3K/Akt and MAPK Signaling Pathways,” Journal of Agricultural and Food Chemistry61, no. 7 (2013): 1509–1520.

[67] S.-Y. Yu, C.-H. Liao, M.-H. Chien, T.-Y. Tsai, J.-K. Lin, and M.-S. Weng, “Induction of p21Waf1/Cip1 by Garcinol via Downregulation of p38-MAPK Signaling in p53-independent H1299 Lung Cancer,” Journal of Agricultural and Food Chemistry62, no. 9 (2014): 2085–2095.

[68] A. I. Ferrer, J. R. Trinidad, O. Sandiford, J.-P. Etchegaray, and P. Rameshwar, “Epigenetic Dynamics in Cancer Stem Cell Dormancy,” Cancer and Metastasis Reviews39 (2020): 721–738.

[69] A. L. Parker and T. R. Cox, “The Role of the ECM in Lung Cancer Dormancy and Outgrowth,” Frontiers in Oncology10 (2020): 567139.

[70] J. He, Y. Zhou, and L. Sun, “Emerging Mechanisms of the Unfolded Protein Response in Therapeutic Resistance: From Chemotherapy to Immunotherapy,” Cell Communication and Signaling22, no. 1 (2024): 89.

[71] E. Madden, S. E. Logue, S. J. Healy, S. Manie, and A. Samali, “The Role of the Unfolded Protein Response in Cancer Progression: From Oncogenesis to Chemoresistance,” Biology of the Cell111, no. 1 (2019): 1–17.

[72] J. Park, K. Lee, K. Kim, and S.-J. Yi, “The Role of Histone Modifications: From Neurodevelopment to Neurodiseases,” Signal Transduction and Targeted Therapy7, no. 1 (2022): 217.

[73] Y. Xiao, M. Hassani, M. B. Moghaddam, A. Fazilat, M. Ojarudi, and M. Valilo, “Contribution of Tumor Microenvironment (TME) to Tumor Apoptosis, Angiogenesis, Metastasis, and Drug Resistance,” Medical Oncology42, no. 4 (2025): 108.

[74] R. Paul, J. F. Dorsey, and Y. Fan, “Cell Plasticity, Senescence, and Quiescence in Cancer Stem Cells: Biological and Therapeutic Implications,” Pharmacology & Therapeutics231 (2022): 107985.

[75] M. Tufail, C.-H. Jiang, and N. Li, “Tumor Dormancy and Relapse: Understanding the Molecular Mechanisms of Cancer Recurrence,” Military Medical Research12, no. 1 (2025): 7.

[76] K. Truskowski, S. R. Amend, and K. J. Pienta, “Dormant Cancer Cells: Programmed Quiescence, Senescence, or Both?,” Cancer and Metastasis Reviews42, no. 1 (2023): 37–47.

[77] P. Lorenc, A. Sikorska, S. Molenda, N. Guzniczak, H. Dams-Kozlowska, and A. Florczak, “Physiological and Tumor-Associated Angiogenesis: Key Factors and Therapy Targeting VEGF/VEGFR Pathway,” Biomedicine & Pharmacotherapy180 (2024): 117585.

[78] X. Liu, J. Zhang, T. Yi, et al., “Decoding Tumor Angiogenesis: Pathways, Mechanisms, and Future Directions in Anti-Cancer Strategies,” Biomarker Research13, no. 1 (2025): 62.

[79] P. Peng, S. Qin, L. Li, et al., “Epigenetic Remodeling Under Oxidative Stress: Mechanisms Driving Tumor Metastasis,” MedComm—Oncology3, no. 4 (2024): e70000.

[80] F. Yang, G. Lee, and Y. Fan, “Navigating Tumor Angiogenesis: Therapeutic Perspectives and Myeloid Cell Regulation Mechanism,” Angiogenesis27, no. 3 (2024): 333–349.

[81] R. Batlle, E. Andrés, L. Gonzalez, et al., “Regulation of Tumor Angiogenesis and Mesenchymal–Endothelial Transition by p38α Through TGF-β and JNK Signaling,” Nature Communications10, no. 1 (2019): 3071.

[82] V. Baeriswyl and G. Christofori, “The Angiogenic Switch in Carcinogenesis,” Seminars in Cancer Biology19, no. 5 (2009): 329–337.

[83] R. Lugano, M. Ramachandran, and A. Dimberg, “Tumor Angiogenesis: Causes, Consequences, Challenges and Opportunities,” Cellular and Molecular Life Sciences77 (2020): 1745–1770.

[84] A. Wicki and G. Christofori, “The Angiogenic Switch in Tumorigenesis.” Tumor Angiogenesis: Basic Mechanisms and Cancer Therapy (Springer, 2008), 67–88.

[85] G. Natale and G. Bocci, “Tumor Dormancy, Angiogenesis and Metronomic Chemotherapy,” in Tumor Dormancy and Recurrence: Cancer Drug Discovery and Development, ed. Y. Wang and F. Crea (Humana Press, 2017), 31–49, https://doi.org/10.1007/978-3-319-59242-8_3.

[86] Y. Wang, L. Wang, Y. Wei, et al., “Advances in the Molecular Regulation Mechanism of Tumor Dormancy and Its Therapeutic Strategy,” Discover Oncology15, no. 1 (2024): 184.

[87] M. S. Rogers, K. Novak, D. Zurakowski, et al., “Spontaneous Reversion of the Angiogenic Phenotype to a Nonangiogenic and Dormant State in Human Tumors,” Molecular Cancer Research12, no. 5 (2014): 754–764.

[88] S. Wang and S.-Y. Lin, “Tumor Dormancy: Potential Therapeutic Target in Tumor Recurrence and Metastasis Prevention,” Experimental Hematology & Oncology2 (2013): 29.

[89] A. Corthay, T. Bakacs, G. Thangavelu, and C. C. Anderson, “Tackling Cancer Cell Dormancy: Insights From Immune Models, and Transplantation,” Seminars in Cancer Biology78 (2022): 5–16.

[90] M. W. L. Teng, J. B. Swann, C. M. Koebel, R. D. Schreiber, and M. J. Smyth, “Immune-Mediated Dormancy: An Equilibrium With Cancer,” Journal of Leukocyte Biology84, no. 4 (2008): 988–993.

[91] I. Romero, F. Garrido, and A. M. Garcia-Lora, “Metastases in Immune-Mediated Dormancy: A New Opportunity for Targeting Cancer,” Cancer Research74, no. 23 (2014): 6750–6757.

[92] B. I. Pereira, O. P. Devine, M. Vukmanovic-Stejic, et al., “Senescent Cells Evade Immune Clearance via HLA-E-Mediated NK and CD8⁺ T Cell Inhibition,” Nature Communications10, no. 1 (2019): 2387.

[93] Q. Wang, S. Chen, Z. Guo, S. Xia, and M. Zhang, “Nk-Like CD8 T Cell: One Potential Evolutionary Continuum Between Adaptive Memory and Innate Immunity,” Clinical and Experimental Immunology217, no. 2 (2024): 136–150.

[94] J. Rosenberg and J. Huang, “CD8+ T Cells and NK Cells: Parallel and Complementary Soldiers of Immunotherapy,” Current Opinion in Chemical Engineering19 (2018): 9–20.

[95] S. P. Castillo, F. Galvez-Cancino, J. Liu, S. M. Pollard, S. A. Quezada, and Y. Yuan, “The Tumour Ecology of Quiescence: Niches Across Scales of Complexity,” Seminars in Cancer Biology92 (2023): 139–149.

[96] P. Wawrzyniak and M. L. Hartman, “Dual Role of Interferon-Gamma in the Response of Melanoma Patients to Immunotherapy With Immune Checkpoint Inhibitors,” Molecular Cancer24, no. 1 (2025): 89.

[97] J. M. Mazet, J. N. Mahale, O. Tong, et al., “IFNγ Signaling in Cytotoxic T Cells Restricts Anti-Tumor Responses by Inhibiting the Maintenance and Diversity of Intra-Tumoral Stem-Like T Cells,” Nature Communications14, no. 1 (2023): 321.

[98] D. Jorgovanovic, M. Song, L. Wang, and Y. Zhang, “Roles of IFN-γ in Tumor Progression and Regression: A Review,” Biomarker Research8 (2020): 49.

[99] Y. Liu, X. Liang, X. Yin, et al., “Blockade of IDO-Kynurenine-AhR Metabolic Circuitry Abrogates IFN-γ-Induced Immunologic Dormancy of Tumor-Repopulating Cells,” Nature Communications8, no. 1 (2017): 15207.

[100] H. Anzai, S. Yoshimoto, K. Okamura, A. Hiraki, and S. Hashimoto, “IDO1-Mediated Trp-Kynurenine-AhR Signal Activation Induces Stemness and Tumor Dormancy in Oral Squamous Cell Carcinomas,” Oral Science International19, no. 1 (2022): 31–43.

[101] Y. Tie, F. Tang, D. Peng, Y. Zhang, and H. Shi, “TGF-Beta Signal Transduction: Biology, Function and Therapy for Diseases,” Molecular Biomedicine3, no. 1 (2022): 45.

[102] C. Prunier, D. Baker, P. Ten Dijke, and L. Ritsma, “TGF-β Family Signaling Pathways in Cellular Dormancy,” Trends in Cancer5, no. 1 (2019): 66–78.

[103] A. Rodríguez-García, P. Samsó, P. Fontova, et al., “TGF-β1 Targets Smad, p38 MAPK, and PI 3K/Akt Signaling Pathways to Induce PFKFB 3 Gene Expression and Glycolysis in Glioblastoma Cells,” FEBS Journal284, no. 20 (2017): 3437–3454.

[104] X. Gao, M. Zhang, Y. Tang, and X. Liang, “Cancer Cell Dormancy: Mechanisms and Implications of Cancer Recurrence and Metastasis,” OncoTargets and Therapy10 (2017): 5219–5228.

[105] A. S. Yadav, P. R. Pandey, R. Butti, et al., “The Biology and Therapeutic Implications of Tumor Dormancy and Reactivation,” Frontiers in Oncology8 (2018): 72.

[106] A. Bhatia and Y. Kumar, “Cancer Immunoediting: Immunosurveillance, Immune Equilibrium, and Immune Escape,” in Cancer Immunology, ed. N. Rezaei (Springer, 2020), 195–208, https://doi.org/10.1007/978-3-030-30845-2_16.

[107] L. Meng, H. Wu, J. Wu, et al., “Mechanisms of Immune Checkpoint Inhibitors: Insights Into the Regulation of Circular RNAS Involved in Cancer Hallmarks,” Cell Death & Disease15, no. 1 (2024): 3.

[108] X. Lin, K. Kang, P. Chen, et al., “Regulatory Mechanisms of PD-1/PD-L1 in Cancers,” Molecular Cancer23, no. 1 (2024): 108.

[109] A. Zabeti Touchaei and S. Vahidi, “MicroRNAs as Regulators of Immune Checkpoints in Cancer Immunotherapy: Targeting PD-1/PD-L1 and CTLA-4 Pathways,” Cancer Cell International24, no. 1 (2024): 102.

[110] K. Kilian, C. Fischbach, and E. L. S. Fong, “Engineered Biomaterials for Developing the Next Generation of In Vitro Tumor Models,” Advanced Healthcare Materials12 (2023): 2300411.

[111] R. Pradhan, A. Kundu, and C. N. Kundu, “The Cytokines in Tumor Microenvironment: From Cancer Initiation-Elongation-Progression to Metastatic Outgrowth,” Critical Reviews in Oncology/Hematology196 (2024): 104311.

[112] A. Mukherjee and J. J. Bravo-Cordero, “Regulation of Dormancy During Tumor Dissemination: The Role of the ECM,” Cancer and Metastasis Reviews42, no. 1 (2023): 99–112.

[113] S. Sharma, B. J. Rodems, C. D. Baker, et al., “Taurine From Tumour Niche Drives Glycolysis to Promote Leukaemogenesis,” Nature644 (2025): 263–272.

[114] Y. Jiao, Y. Yu, M. Zheng, et al., “Dormant Cancer Cells and Polyploid Giant Cancer Cells: The Roots of Cancer Recurrence and Metastasis,” Clinical and Translational Medicine14, no. 2 (2024): e1567.

[115] C. Biray Avci, B. Goker Bagca, M. Nikanfar, L. S. Takanlou, M. S. Takanlou, and A. Nourazarian, “Tumor Microenvironment and Cancer Metastasis: Molecular Mechanisms and Therapeutic Implications,” Frontiers in Pharmacology15 (2024): 1442888.

[116] S. A. Desai, V. P. Patel, K. P. Bhosle, S. D. Nagare, and K. C. Thombare, “The Tumor Microenvironment: Shaping Cancer Progression and Treatment Response,” Journal of Chemotherapy37, no. 1 (2025): 15–44.

[117] S. Ji, Y. Shi, and B. Yin, “Macrophage Barrier in the Tumor Microenvironment and Potential Clinical Applications,” Cell Communication and Signaling22, no. 1 (2024): 74.

[118] A. Glaviano, H. S.-H. Lau, L. M. Carter, et al., “Harnessing the Tumor Microenvironment: Targeted Cancer Therapies Through Modulation of Epithelial-Mesenchymal Transition,” Journal of Hematology & Oncology18, no. 1 (2025): 6.

[119] T. Bui, Y. Gu, F. Ancot, V. Sanguin-Gendreau, D. Zuo, and W. J. Muller, “Emergence of β1 Integrin-Deficient Breast Tumours From Dormancy Involves Both Inactivation of p53 and Generation of a Permissive Tumour Microenvironment,” Oncogene41, no. 4 (2022): 527–537.

[120] J. R. W. Conway, O. Joshi, J. Kaivola, et al., “Dynamic Regulation of Integrin β1 Phosphorylation Supports Invasion of Breast Cancer Cells,” Nature Cell Biology27 (2025): 1021–1034.

[121] Y. Zhao, X. Zhang, X. Zhang, G. Shen, W. Li, and Q. Wang, “Integrinβ1/FAK/ERK Signalling Pathway Is Essential for Chinese Mitten Crab Eriocheir Sinensis Hemocyte Survival,” Fish & Shellfish Immunology132 (2023): 108473.

[122] D. Barkan and A. F. Chambers, “β1-Integrin: A Potential Therapeutic Target in the Battle Against Cancer Recurrence,” Clinical Cancer Research17, no. 23 (2011): 7219–7223.

[123] L. E. Barney, C. L. Hall, A. D. Schwartz, et al., “Tumor Cell–Organized Fibronectin Maintenance of a Dormant Breast Cancer Population,” Science Advances6, no. 11 (2020): eaaz4157.

[124] L. Jingyuan, L. Yu, J. Hong, et al., “Matrix Stiffness Induces an Invasive-Dormant Subpopulation via cGAS-STING Axis in Oral Cancer,” Translational Oncology33 (2023): 101681.

[125] Z. Fang, T. Zhang, N. Dizeyi, et al., “Androgen Receptor Enhances p27 Degradation in Prostate Cancer Cells Through Rapid and Selective TORC2 Activation,” Journal of Biological Chemistry287, no. 3 (2012): 2090–2098.

[126] D. B. Widner, S. H. Park, M. R. Eber, and Y. Shiozawa, “Interactions Between Disseminated Tumor Cells and Bone Marrow Stromal Cells Regulate Tumor Dormancy,” Current Osteoporosis Reports16 (2018): 596–602.

[127] R. Dai, M. Liu, X. Xiang, Z. Xi, and H. Xu, “Osteoblasts and Osteoclasts: An Important Switch of Tumour Cell Dormancy During Bone Metastasis,” Journal of Experimental & Clinical Cancer Research41, no. 1 (2022): 316.

[128] J. Zarrer and H. Taipaleenmäki, “The Osteoblast in Regulation of Tumor Cell Dormancy and Bone Metastasis,” Journal of Bone Oncology45 (2024): 100597.

[129] C. M. Ghajar, H. Peinado, H. Mori, et al., “The Perivascular Niche Regulates Breast Tumour Dormancy,” Nature Cell Biology15, no. 7 (2013): 807–817.

[130] A. Nowosad, J.-C. Marine, and P. Karras, “Perivascular Niches: Critical Hubs in Cancer Evolution,” Trends in Cancer9, no. 11 (2023): 897–910.

[131] S. Drapela, B. M. Garcia, A. P. Gomes, and A. L. Correia, “Metabolic Landscape of Disseminated Cancer Dormancy.” Trends Cancer11, 4 (2024), 321–333.

[132] K. E. Lee, “Hypoxia as a Regulator of Tumor Stroma and Metastasis,” American Journal of Physiology—Cell Physiology324, no. 1 (2023): C10–C13.

[133] A. Varveri, M. Papadopoulou, Z. Papadovasilakis, et al., “Immunological Synapse Formation Between T Regulatory Cells and Cancer-Associated Fibroblasts Promotes Tumour Development,” Nature Communications15, no. 1 (2024): 4988.

[134] Y. Lin, Q. Cai, Y. Chen, et al., “CAFs Shape Myeloid-Derived Suppressor Cells to Promote Stemness of Intrahepatic Cholangiocarcinoma Through 5-Lipoxygenase,” Hepatology75, no. 1 (2022): 28–42.

[135] A. Adam-Artigues, L. E. Valencia Salazar, and J. A. Aguirre-Ghiso, “Immune Evasion by Dormant Disseminated Cancer Cells: A Fermi Paradox?,” Cancer Cell42, no. 1 (2024): 13–15.

[136] M. S. Sosa, P. Bragado, and J. A. Aguirre-Ghiso, “Mechanisms of Disseminated Cancer Cell Dormancy: an Awakening Field,” Nature Reviews Cancer14, no. 9 (2014): 611–622.

[137] N. Linde, G. Fluegen, and J. Aguirre-Ghiso, “The Relationship Between Dormant Cancer Cells and Their Microenvironment,” Advances in Cancer Research132 (2016): 45–71.

[138] M. T. Blasco, I. Espuny, and R. R. Gomis, “Ecology and Evolution of Dormant Metastasis,” Trends in Cancer8, no. 7 (2022): 570–582.

[139] R. Siddhartha and M. Garg, “Interplay Between Extracellular Matrix Remodeling and Angiogenesis in Tumor Ecosystem,” Molecular Cancer Therapeutics22, no. 3 (2023): 291–305.

[140] L. Patras, D. Paul, and I. R. Matei, “Weaving the Nest: Extracellular Matrix Roles in Pre-Metastatic Niche Formation,” Frontiers in Oncology13 (2023): 1163786.

[141] M. De Palma, D. Biziato, and T. V. Petrova, “Microenvironmental Regulation of Tumour Angiogenesis,” Nature Reviews Cancer17, no. 8 (2017): 457–474.

[142] Y. Yang and Y. Cao, “The Impact of VEGF on Cancer Metastasis and Systemic Disease,” Seminars in Cancer Biology86 (2022): 251–261.

[143] A. Shafqat, M. H. Omer, E. N. Ahmed, et al., “Reprogramming the Immunosuppressive Tumor Microenvironment: Exploiting Angiogenesis and Thrombosis to Enhance Immunotherapy,” Frontiers in Immunology14 (2023): 1200941.

[144] R. D. Meyer, X. Zou, M. Ali, et al., “TMIGD1 Acts as a Tumor Suppressor Through Regulation of p21Cip1/p27Kip1 in Renal Cancer,” Oncotarget9, no. 11 (2017): 9672–9684.

[145] W. Yan, X. Wang, W. Wang, et al., “The p38/MAPK Pathway as a Therapeutic Target to Prevent Therapeutic Escape of Breast Cancer Stem Cells,” Science China Life Sciences67, no. 9 (2024): 1867–1880.

[146] R. B. Kargbo, “Targeting Oncogenic Pathways: Advances in KRAS, CDK, EGFR, and PROTAC-Based Therapies,” ACS Medicinal Chemistry Letters16 (2025): 523–525.

[147] K. Leelahavanichkul, P. Amornphimoltham, A. A. Molinolo, J. R. Basile, S. Koontongkaew, and J. S. Gutkind, “A Role for p38 MAPK in Head and Neck Cancer Cell Growth and Tumor-Induced Angiogenesis and Lymphangiogenesis,” Molecular Oncology8, no. 1 (2014): 105–118.

[148] P. Mohammadzadeh, P. Sen, A. A. Zourelidis, and J. A. Califano, “Evaluation of the Effects of THC on Migration, Proliferation, and Tumor Growth in HPV-Negative HNSCC,” Journal of Clinical Oncology43 (2025): e18062.

[149] S. Kudaravalli, P. den Hollander, and S. A. Mani, “Role of p38 MAP Kinase in Cancer Stem Cells and Metastasis,” Oncogene41, no. 23 (2022): 3177–3185.

[150] C. Li, D. Cheng, and P. Li, “Androgen Receptor Dynamics in Prostate Cancer: From Disease Progression to Treatment Resistance,” Frontiers in Oncology15 (2025): 1542811.

[151] R. Safi, S. E. Wardell, P. Watkinson, et al., “Androgen Receptor Monomers and Dimers Regulate Opposing Biological Processes in Prostate Cancer Cells,” Nature Communications15, no. 1 (2024): 7675.

[152] M. Roerden and S. Spranger, “Cancer Immune Evasion, Immunoediting and Intratumour Heterogeneity,” Nature Reviews Immunology25 (2025): 353–369.

[153] E. T. Goddard, I. Bozic, S. R. Riddell, and C. M. Ghajar, “Dormant Tumour Cells, Their Niches and the Influence of Immunity,” Nature Cell Biology20, no. 11 (2018): 1240–1249.

[154] Z. Lu, C. Zhang, J. Zhang, W. Su, G. Wang, and Z. Wang, “The Kynurenine Pathway and Indole Pathway in Tryptophan Metabolism Influence Tumor Progression,” Cancer Medicine14, no. 6 (2025): e70703.

[155] K. K. Payne, “Cellular Stress Responses and Metabolic Reprogramming in Cancer Progression and Dormancy,” Seminars in Cancer Biology78 (2022): 45–48.

[156] S. Bartlome and C. C. Berry, “Recent Insights Into the Effects of Metabolism on Breast Cancer Cell Dormancy,” British Journal of Cancer127, no. 8 (2022): 1385–1393.

[157] Z. Wu, J. Wu, Q. Zhao, S. Fu, and J. Jin, “Emerging Roles of Aerobic Glycolysis in Breast Cancer,” Clinical and Translational Oncology22, no. 5 (2020): 631–646.

[158] E. S. Saheed, R. F. Aromolaran, A. D. Atoyebi, F. C. Adeleke, A. I. Otuyalo, and P. K. Edozie, “Mechanism of the Warburg Effect and Its Role in Breast Cancer Immunotherapy,” Discover Medicine1, no. 1 (2024): 110.

[159] R. Qin, X. Fan, Y. Huang, et al., “Role of Glucose Metabolic Reprogramming in Colorectal Cancer Progression and Drug Resistance,” Translational Oncology50 (2024): 102156.

[160] M. C. Heinz, N. A. Peters, K. C. Oost, et al., “Liver Colonization by Colorectal Cancer Metastases Requires YAP-Controlled Plasticity at the Micrometastatic Stage,” Cancer Research82, no. 10 (2022): 1953–1968.

[161] R. Sun, Z. Lin, X. Wang, et al., “AADAC Protects Colorectal Cancer Liver Colonization From Ferroptosis Through SLC7A11-Dependent Inhibition of Lipid Peroxidation,” Journal of Experimental & Clinical Cancer Research41, no. 1 (2022): 284.

[162] C. Papadaki, M. Stratigos, G. Markakis, et al., “Circulating MicroRNAs in the Early Prediction of Disease Recurrence in Primary Breast Cancer,” Breast Cancer Research20 (2018): 72.

[163] J. Zhuang, Q. Huo, F. Yang, and N. Xie, “Perspectives on the Role of Histone Modification in Breast Cancer Progression and the Advanced Technological Tools to Study Epigenetic Determinants of Metastasis,” Frontiers in Genetics11 (2020): 603552.

[164] F. Rago, G. Elliott, A. Li, et al., “The Discovery of SWI/SNF Chromatin Remodeling Activity as a Novel and Targetable Dependency in Uveal Melanoma,” Molecular Cancer Therapeutics19, no. 10 (2020): 2186–2195.

[165] R. Liang and G. Song, “Matrix Stiffness-Driven Cancer Progression and the Targeted Therapeutic Strategy,” Mechanobiology in Medicine1, no. 2 (2023): 100013.

[166] H. Lee, S. W. Cho, H. S. Cha, K. Tae, and C. Y. Choi, “Transient Activation of YAP/TAZ Confers Resistance to Morusin-Induced Apoptosis,” BMC Molecular and Cell Biology26, no. 1 (2025): 4.

[167] D. He, Q. Wu, P. Tian, et al., “Chemotherapy Awakens Dormant Cancer Cells in Lung by Inducing Neutrophil Extracellular Traps,” Cancer Cell43, no. 9 (2025): 1622–1636.e7.

[168] L. Wang, Q. Peng, N. Yin, et al., “Chromatin Accessibility Regulates Chemotherapy-Induced Dormancy and Reactivation,” Molecular Therapy—Nucleic Acids26 (2021): 269–279.

[169] Y. Du, P. Gupta, S. Qin, and M. Sieber, “The Role of Metabolism in Cellular Quiescence,” Journal of Cell Science136, no. 16 (2023): jcs260787.

[170] G. L. Ismaeel, A. H. Abdul-Hussein, H. M. Qasim, et al., “Therapeutic Targeting of Dormant Cancer Stem Cells in Solid Tumors,” Gene Reports30 (2023): 101717.

[171] A. Zafar, S. Khatoon, M. J. Khan, J. Abu, and A. Naeem, “Advancements and Limitations in Traditional Anti-Cancer Therapies: A Comprehensive Review of Surgery, Chemotherapy, Radiation Therapy, and Hormonal Therapy,” Discover Oncology16, no. 1 (2025): 607.

[172] U. Anand, A. Dey, A. K. S. Chandel, et al., “Cancer Chemotherapy and Beyond: Current Status, Drug Candidates, Associated Risks and Progress in Targeted Therapeutics,” Genes & Diseases10, no. 4 (2023): 1367–1401.

[173] A. Ring, M. Spataro, A. Wicki, and N. Aceto, “Clinical and Biological Aspects of Disseminated Tumor Cells and Dormancy in Breast Cancer,” Frontiers in Cell and Developmental Biology10 (2022): 929893.

[174] G. G. Bushnell, A. P. Deshmukh, P. den Hollander, et al., “Breast Cancer Dormancy: Need for Clinically Relevant Models to Address Current Gaps in Knowledge,” NPJ Breast Cancer7, no. 1 (2021): 66.

[175] D. Uzuner, Y. Akkoç, N. Peker, P. Pir, D. Gözüaçık, and T. Çakır, “Transcriptional Landscape of Cellular Networks Reveal Interactions Driving the Dormancy Mechanisms in Cancer,” Scientific Reports11, no. 1 (2021): 15806.

[176] Y. Yang, W.-J. Meng, and Z.-Q. Wang, “Cancer Stem Cells and the Tumor Microenvironment in Gastric Cancer,” Frontiers in Oncology11 (2022): 803974.

[177] T. Rogkoti, H. Donnelly, M. J. Dalby, and M. Salmeron-Sanchez, “Mechanical Signatures and Models of the Bone Marrow Niche,” Nature Reviews Bioengineering3 (2025): 697–713.

[178] Z. Mai, Y. Lin, P. Lin, X. Zhao, and L. Cui, “Modulating Extracellular Matrix Stiffness: A Strategic Approach to Boost Cancer Immunotherapy,” Cell Death & Disease15, no. 5 (2024): 307.

[179] A. Pérez-González, K. Bévant, and C. Blanpain, “Cancer Cell Plasticity During Tumor Progression, Metastasis and Response to Therapy,” Nature Cancer4, no. 8 (2023): 1063–1082.

[180] M. Labrie, J. S. Brugge, G. B. Mills, and I. K. Zervantonakis, “Therapy Resistance: Opportunities Created by Adaptive Responses to Targeted Therapies in Cancer,” Nature Reviews Cancer22, no. 6 (2022): 323–339.

[181] S. Talukdar, P. Bhoopathi, L. Emdad, S. Das, D. Sarkar, and P. B. Fisher, “Dormancy and Cancer Stem Cells: An Enigma for Cancer Therapeutic Targeting,” Advances in Cancer Research141 (2019): 43–84.

[182] Y. El Yousfi, F. J. Fernández-Farrán, F. J. Oliver, A. López-Rivas, and R. Yerbes, “Regulation of ER Stress-Induced Apoptotic and Inflammatory Responses via YAP/TAZ-Mediated Control of the TRAIL-R2/DR5 Signaling Pathway,” Cell Death Discovery11, no. 1 (2025): 42.

[183] L. Ruan and L. Wang, “Adoptive Cell Therapy Against Tumor Immune Evasion: Mechanisms, Innovations, and Future Directions,” Frontiers in Oncology15 (2025): 1530541.

[184] S. Tau and T. W. Miller, “The Role of Cancer Cell Bioenergetics in Dormancy and Drug Resistance,” Cancer and Metastasis Reviews42, no. 1 (2023): 87–98.

[185] L. Marrone, S. Romano, C. Malasomma, et al., “Metabolic Vulnerability of Cancer Stem Cells and Their Niche,” Frontiers in Pharmacology15 (2024): 1375993.

[186] H. Zhang, S. Li, D. Wang, et al., “Metabolic Reprogramming and Immune Evasion: The Interplay in the Tumor Microenvironment,” Biomarker Research12, no. 1 (2024): 96.

[187] C. Mancini, G. Lori, E. Pranzini, and M. L. Taddei, “Metabolic Challengers Selecting Tumor-Persistent Cells,” Trends in Endocrinology & Metabolism35, no. 3 (2024): 263–276.

[188] M. Zhang and H. Xu, “Peptide-Assembled Nanoparticles Targeting Tumor Cells and Tumor Microenvironment for Cancer Therapy,” Frontiers in Chemistry11 (2023): 1115495.

[189] V. B. Kumar, B. Ozguney, A. Vlachou, Y. Chen, E. Gazit, and P. Tamamis, “Peptide Self-Assembled Nanocarriers for Cancer Drug Delivery,” Journal of Physical Chemistry B127, no. 9 (2023): 1857–1871.

[190] X. Li, F. Yang, M. Wang, et al., “Unleashing the Power of Peptides in Prostate Cancer Immunotherapy: Mechanism, Facts and Perspectives,” Frontiers in Pharmacology16 (2025): 1478331.

[191] A. R. Aleem, W. Ali, H. Pan, et al., “Multifunctional Peptide- and Natural Polymer-Based Smart Biomaterials: Synthetic Approaches and Cancer Treatment Applications,” Coordination Chemistry Reviews544 (2025): 216980.

[192] L. Wang, N. Wang, W. Zhang, et al., “Therapeutic Peptides: Current Applications and Future Directions,” Signal Transduction and Targeted Therapy7, no. 3 (2022): 48.

[193] A. Naeem, N. Noureen, S. K. Al-Naemi, J. A. Al-Emadi, and M. J. Khan, “Computational Design of Anti-Cancer Peptides Tailored to Target Specific Tumor Markers,” BMC Chemistry18, no. 1 (2024): 39.

[194] Q. Zhang, N. Liu, J. Wang, et al., “The Recent Advance of Cell-Penetrating and Tumor-Targeting Peptides as Drug Delivery Systems Based on Tumor Microenvironment,” Molecular Pharmaceutics20, no. 2 (2023): 789–809.

[195] Y. Wu, L. Qin, J. Wang, et al., “Stabilized iRGD Modification Enhances NY-ESO-1 TCR-T Infiltration in Solid Tumors and Synergizes With PD-1 Blockade,” Cancer Immunology, Immunotherapy74, no. 7 (2025): 226.

[196] T. Singh, T. W. Kim, A. S. N. Murthy, et al., “Tumor–Homing Peptide iRGD-Conjugate Enhances Tumor Accumulation of Camptothecin for Colon Cancer Therapy,” European Journal of Medicinal Chemistry265 (2024): 116050.

[197] A. M. Gasparri, A. Pocaterra, B. Colombo, et al., “Blockade of αΑ_vβ₆ and αΑ_vβ₈ Integrins With a Chromogranin A-Derived Peptide Inhibits TGFβ Activation in Tumors and Suppresses Tumor Growth,” Journal of Experimental & Clinical Cancer Research44, no. 1 (2025): 88.

[198] C. Liu, A. Hu, H. Chen, et al., “The Osteogenic Niche-Targeted Arsenic Nanoparticles Prevent Colonization of Disseminated Breast Tumor Cells in the Bone,” Acta Pharmaceutica Sinica B12, no. 1 (2022): 364–377.

[199] X. Li, Y. Liang, C. Lian, et al., “CST6 Protein and Peptides Inhibit Breast Cancer Bone Metastasis by Suppressing CTSB Activity and Osteoclastogenesis,” Theranostics11, no. 20 (2021): 9821–9832.

[200] Y. Wang, J. Liu, Y. Gong, et al., “Bone Marrow Disseminated Tumor Cell Detection Is Beneficial for the Early Finding of Bone Metastasis and Prognosis,” Diagnostics14, no. 15 (2024): 1629.

[201] O. Gilon, K. Weidenfeld, H. Samara, et al., “Abstract A074: Targeting Dormant Disseminated Tumor Cells and Their Permissive Niche by Pro-Resolving Mediators Derived From Resolution-Phase Macrophages,” supplement, Cancer Research84, no. 3_Suppl_1 (2024): A074.

[202] M. Serulla, G. Ichim, F. Stojceski, et al., “TAT-RasGAP_317-326 Kills Cells by Targeting Inner-Leaflet–Enriched Phospholipids,” Proceedings of the National Academy of Sciences117, no. 50 (2020): 31871–31881.

[203] X. Chen, C. Hu, Y. Zhang, et al., “Anticancer Activity and Mechanism of Action of kla-TAT Peptide,” International Journal of Peptide Research and Therapeutics26 (2020): 2285–2296.

[204] Q. Xu, F. Zhu, Y. Pan, et al., “HIV Tat-Conjugated Histone H3 Peptides Induce Tumor Cell Death via Cellular Stress Responses,” Human Gene Therapy34, no. 1–2 (2023): 42–55.

[205] Y. S. Lee, M. J. Lee, and W. J. Shon, “Abstract A029: Identification of Cancer-Specific CPP From Human Telomerase Peptide Library and Its Drug Delivery Potential in Anti-Cancer Strategy,” Molecular Cancer Therapeutics22, no. 12 (2023): A029.

[206] D. B. Tran, K. Christov, S. Mander, et al., “Intracellular Redistribution of Cell-Penetrating Peptide p28: A Mechanism for Enhanced Anti-Cancer Activity,” Journal of Controlled Release382 (2025): 113660.

[207] F. Huang, Q. Shu, Z. Qin, et al., “Anticancer Actions of Azurin and Its Derived Peptide p28,” Protein Journal39 (2020): 182–189.

[208] G. Guidotti, L. Brambilla, and D. Rossi, “Cell-Penetrating Peptides: From Basic Research to Clinics,” Trends in Pharmacological Sciences38, no. 4 (2017): 406–424.

[209] Y. Y. Xu, X. W. Cao, L. Y. Fu, T. Z. Zhang, F. J. Wang, and J. Zhao, “Screening and Characterization of a Novel High-Efficiency Tumor-Homing Cell-Penetrating Peptide From the Buffalo Cathelicidin Family,” Journal of Peptide Science25, no. 9 (2019): e3201.

[210] M.-C. Wu, E. Y. Wang, and T. W. Lai, “TAT Peptide at Treatment-Level Concentrations Crossed Brain Endothelial Cell Monolayer Independent of Receptor-Mediated Endocytosis or Peptide-Inflicted Barrier Disruption,” PLoS One18, no. 10 (2023): e0292681.

[211] M. Yu, X. Li, X. Huang, J. Zhang, Y. Zhang, and H. Wang, “New Cell-Penetrating Peptide (KRP) With Multiple Physicochemical Properties Endows Doxorubicin With Tumor Targeting and Improves Its Therapeutic Index,” ACS Applied Materials & Interfaces11, no. 2 (2018): 2448–2458.

[212] B. Ghaemi, S. Tanwar, A. Singh, et al., “Cell-Penetrating and Enzyme-Responsive Peptides for Targeted Cancer Therapy: Role of Arginine Residue Length on Cell Penetration and In Vivo Systemic Toxicity,” ACS Applied Materials & Interfaces16, no. 9 (2024): 11159–11171.

[213] M. Wang, J. Liu, M. Xia, et al., “Peptide-Drug Conjugates: A New Paradigm for Targeted Cancer Therapy,” European Journal of Medicinal Chemistry265 (2024): 116119.

[214] G. Mező, J. Gomena, I. Ranđelović, et al., “Oxime-Linked Peptide–Daunomycin Conjugates as Good Tools for Selection of Suitable Homing Devices in Targeted Tumor Therapy: An Overview,” International Journal of Molecular Sciences25, no. 3 (2024): 1864.

[215] P. E. Saw, X. Xu, S. Kim, and S. Jon, “Biomedical Applications of a Novel Class of High-Affinity Peptides,” Accounts of Chemical Research54, no. 18 (2021): 3576–3592.

[216] E. I. Vrettos and A. G. Tzakos, “Construction of Peptide-Drug Conjugates for Selective Targeting of Malignant Tumor Cells,” Methods in Molecular Biology2207 (2020): 327–338.

[217] E. I. Vrettos, G. Mező, and A. G. Tzakos, “On the Design Principles of Peptide–Drug Conjugates for Targeted Drug Delivery to the Malignant Tumor Site,” Beilstein Journal of Organic Chemistry14, no. 1 (2018): 930–954.

[218] I. R. Palombi, A. M. White, Y. Koda, D. J. Craik, N. Lawrence, and L. R. Malins, “Synthesis and Investigation of Peptide–Drug Conjugates Comprising Camptothecin and a Human Protein-Derived Cell-Penetrating Peptide,” Chemical Biology & Drug Design105, no. 1 (2025): e70051.

[219] D. Wang, F. Yin, Z. Li, Y. Zhang, and C. Shi, “Current Progress and Remaining Challenges of Peptide–Drug Conjugates (PDCs): Next Generation of Antibody-Drug Conjugates (ADCs)?,” Journal of Nanobiotechnology23, no. 1 (2025): 305.

[220] S. F. A. Rizvi, L. Zhang, H. Zhang, and Q. Fang, “Peptide-Drug Conjugates: Design, Chemistry, and Drug Delivery System as a Novel Cancer Theranostic,” ACS Pharmacology & Translational Science7, no. 2 (2024): 309–334.

[221] M. J. Sis, Z. Ye, K. La Costa, and M. J. Webber, “Energy Landscapes of Supramolecular Peptide–Drug Conjugates Directed by Linker Selection and Drug Topology,” ACS Nano16, no. 6 (2022): 9546–9558.

[222] J. Ma, X. Wang, Y. Hu, et al., “Recent Advances in Augmenting the Therapeutic Efficacy of Peptide–Drug Conjugates,” Journal of Medicinal Chemistry68, no. 9 (2025): 9037–9056.

[223] X. Hu, J. Liu, Q. Wang, et al., “Colon Cancer-Cell-Specific Drug Delivery by Gemcitabine Conjugated With Peptide Chain Targeting ENO1,” International Journal of Pharmaceutics673 (2025): 125402.

[224] C. Correia, C. P. R. Xavier, D. Duarte, et al., “Development of Potent CPP6–Gemcitabine Conjugates Against Human Prostate Cancer Cell Line (PC-3),” RSC Medicinal Chemistry11, no. 2 (2020): 268–273.

[225] L. Wang, H. Chen, F. Wang, and X. Zhang, “The Development of Peptide-Drug Conjugates (PDCs) Strategies for Paclitaxel,” Expert Opinion on Drug Delivery19, no. 2 (2022): 147–161.

[226] Y. Li, Q. Feng, Q. Gao, et al., “PTX-RPPR, a Conjugate of Paclitaxel and NRP-1 Peptide Inhibitor to Prevent Tumor Growth and Metastasis,” Biomedicine & Pharmacotherapy178 (2024): 117264.

[227] D. Hua, L. Tang, W. Wang, et al., “Improved Antiglioblastoma Activity and BBB Permeability by Conjugation of Paclitaxel to a Cell-Penetrative MMP-2-Cleavable Peptide,” Advanced Science8, no. 3 (2021): 2001960.

[228] J. Kim, M. K. Shim, Y. Moon, et al., “Cancer Cell-Specific and Pro-Apoptotic SMAC Peptide-Doxorubicin Conjugated Prodrug Encapsulated Aposomes for Synergistic Cancer Immunotherapy,” Journal of Nanobiotechnology22, no. 1 (2024): 109.

[229] M. A. Elsawy, J. K. Wychowaniec, L. A. Castillo Díaz, A. M. Smith, A. F. Miller, and A. Saiani, “Controlling Doxorubicin Release From a Peptide Hydrogel Through Fine-Tuning of Drug–Peptide Fiber Interactions,” Biomacromolecules23, no. 6 (2022): 2624–2634.

[230] C. Diaferia, E. Rosa, A. Accardo, and G. Morelli, “Peptide-Based Hydrogels as Delivery Systems for Doxorubicin,” Journal of Peptide Science28, no. 1 (2022): e3301.

[231] X. Song, K. L. Lan, Y. F. Xue, et al., “Self-Assembled Amphiphilic Camptothecin Nanoparticles With Glutathione-Responsive and Tumor-Targeting Ability for Enhanced Colorectal Cancer Therapy,” Advanced Therapeutics6, no. 11 (2023): 2300174.

[232] Y. Tao, M. Du, M. Zhu, et al., “Antitumor Effect of Peptide–Camptothecin Conjugate Targeting CD133 Protein,” Bioconjugate Chemistry35, no. 11 (2024): 1859–1869.

[233] L. Hou, Y. Hou, Y. Liang, et al., “Anti-Tumor Effects of P-LPK-CPT, a Peptide-Camptothecin Conjugate, in Colorectal Cancer,” Communications Biology5, no. 1 (2022): 1248.

[234] A. A. P. Tripodi, I. Ranđelović, B. Biri-Kovács, B. Szeder, G. Mező, and J. Tóvári, “In Vivo Tumor Growth Inhibition and Antiangiogenic Effect of Cyclic NGR Peptide-Daunorubicin Conjugates Developed for Targeted Drug Delivery,” Pathology & Oncology Research26 (2020): 1879–1892.

[235] Z. Szász, K. N. Enyedi, A. Takács, et al., “Characterisation of the Cell and Molecular Biological Effect of Peptide-Based Daunorubicin Conjugates Developed for Targeting Pancreatic Adenocarcinoma (PANC-1) Cell Line,” Biomedicine & Pharmacotherapy173 (2024): 116293.

[236] Q. Li, Y. Liu, Y. Cheng, et al., “Reduction-Responsive RGD-Docetaxel Conjugate: Synthesis, In Vitro Drug Release and In Vitro Antitumor Activity,” Drug Development Research86, no. 1 (2025): e70043.

[237] B. Wang, D. Tang, J. Cui, H. Jiang, J. Yu, and Z. Guo, “RGD-Based Self-Assembling Nanodrugs for Improved Tumor Therapy,” Frontiers in Pharmacology15 (2024): 1477409.

[238] V. M. D'Amore, G. Donati, E. Lenci, et al., “Molecular View on the iRGD Peptide Binding Mechanism: Implications for Integrin Activity and Selectivity Profiles,” Journal of Chemical Information and Modeling63, no. 20 (2023): 6302–6315.

[239] S. F. A. Rizvi, N. Abbas, H. Zhang, and Q. Fang, “Identification of a pH-Responsive Peptide–Paclitaxel Conjugate as a Novel Drug With Improved Therapeutic Potential,” Journal of Medicinal Chemistry66, no. 12 (2023): 8324–8337.

[240] E. I. Vrettos, T. Karampelas, N. Sayyad, et al., “Development of Programmable Gemcitabine-GnRH Pro-Drugs Bearing Linker Controllable “Click” Oxime Bond Tethers and Preclinical Evaluation Against Prostate Cancer,” European Journal of Medicinal Chemistry211 (2021): 113018.

[241] N. Sayyad, E. I. Vrettos, T. Karampelas, et al., “Development of Bioactive Gemcitabine-D-Lys6-GnRH Prodrugs With Linker-Controllable Drug Release Rate and Enhanced Biopharmaceutical Profile,” European Journal of Medicinal Chemistry166 (2019): 256–266.

[242] O. Argyros, T. Karampelas, X. Asvos, et al., “Peptide–Drug Conjugate GnRH–Sunitinib Targets Angiogenesis Selectively at the Site of Action to Inhibit Tumor Growth,” Cancer Research76, no. 5 (2016): 1181–1192.

[243] D. Fitzgerald, E. C. H. Ho, E. Miller, R. Qiu, and A. Antignani, “Antitumor Activity of Antibody-Drug Conjugates Targeting Cancer-Expressed EGFR in Preclinical Models,” European Journal of Cancer174 (2022): S86–S87.

[244] M. Sharma, D. Panwar, P. Tiwari, et al., “Immobilized Doxorubicin and Ribociclib Carbamate Linkers Encaged in Surface Modified Cubosomes Spatially Target Tumor Reductive Environment to Enhance Antitumor Efficacy,” Biomaterials Advances155 (2023): 213672.

[245] S. Y. Y. Ha, Y. Anami, C. M. Yamazaki, et al., “An Enzymatically Cleavable Tripeptide Linker for Maximizing the Therapeutic Index of Antibody–Drug Conjugates,” Molecular Cancer Therapeutics21, no. 9 (2022): 1449–1461.

[246] X. Li, M. Cheng, Y. Wang, et al., “LC-MS/MS Method for Dual-Ligand Peptide-Drug CBP-1018 and Its Deconjugated Payload MMAE Including Sample Stabilization Strategy for Its MC-Val-Cit-PABC Linker,” Talanta279 (2024): 126596.

[247] B. J. Stenton, B. L. Oliveira, M. J. Matos, L. Sinatra, and G. J. L. Bernardes, “A Thioether-Directed Palladium-Cleavable Linker for Targeted Bioorthogonal Drug Decaging,” Chemical Science9, no. 17 (2018): 4185–4189.

[248] N. M. Grob, D. Häussinger, X. Deupi, R. Schibli, M. Behe, and T. L. Mindt, “Triazolo-Peptidomimetics: Novel Radiolabeled Minigastrin Analogs for Improved Tumor Targeting,” Journal of Medicinal Chemistry63, no. 9 (2020): 4484–4495.

[249] X. Guarrochena, M. Anderla, P. Salomon, et al., “Combination of the Amide-to-Triazole Substitution Strategy With Alternative Structural Modifications for the Metabolic Stabilization of Tumor-Targeting, Radiolabeled Peptides,” Journal of Peptide Science31, no. 1 (2025): e3654.

[250] J. T. W. Tong, M. Sarwar, M. Ahangarpour, et al., “Use of a Cyclic α-Alkylidene-β-Diketone as a Cleavable Linker Strategy for Antibody-Drug Conjugates,” Journal of the American Chemical Society146, no. 34 (2024): 23717–23728.

[251] S. Gayle, R. Aiello, N. Leelatian, et al., “Tumor-Selective, Antigen-Independent Delivery of a pH Sensitive Peptide-Topoisomerase Inhibitor Conjugate Suppresses Tumor Growth Without Systemic Toxicity,” NAR Cancer3, no. 2 (2021): zcab021.

[252] S. Zheng, Y. Cai, Y. Hong, et al., “Legumain/pH Dual-Responsive Lytic Peptide–Paclitaxel Conjugate for Synergistic Cancer Therapy,” Drug Delivery29, no. 1 (2022): 1764–1775.

[253] R. Sun, Y. Zhang, X. Lin, et al., “Aminopeptidase N-Responsive Conjugates With Tunable Charge-Reversal Properties for Highly Efficient Tumor Accumulation and Penetration,” Angewandte Chemie International Edition62, no. 9 (2023): e202217408.

[254] C. Qian, J. Wang, Y. Qian, et al., “Tumor-Cell-Surface Adherable Peptide-Drug Conjugate Prodrug Nanoparticles Inhibit Tumor Metastasis and Augment Treatment Efficacy,” Nano Letters20, no. 6 (2020): 4153–4161.

[255] Z. Wang, J. Guo, J. Sun, et al., “Thermoresponsive and Protease-Cleavable Interferon-Polypeptide Conjugates With Spatiotemporally Programmed Two-Step Release Kinetics for Tumor Therapy,” Advanced Science6, no. 16 (2019): 1900586.

[256] M. Alas, A. Saghaeidehkordi, and K. Kaur, “Peptide–Drug Conjugates With Different Linkers for Cancer Therapy,” Journal of Medicinal Chemistry64, no. 1 (2020): 216–232.

[257] J. Zhou, Z. Xie, J. Wang, et al., “Design, Synthesis and Bioactivity Evaluation of Novel Fusion Peptides and Their CPT Conjugates Inducing Effective Anti-Tumor Responses on HER2 Positive Tumors,” European Journal of Medicinal Chemistry264 (2024): 116032.

[258] Y. Jiang, W. Huang, X. Sun, et al., “DTX-P7, a Peptide–Drug Conjugate, Is Highly Effective for Non-Small Cell Lung Cancer,” Journal of Hematology & Oncology15, no. 1 (2022): 73.

[259] Y.-S. Zhu, K. Tang, and J. Lv, “Peptide–Drug Conjugate-Based Novel Molecular Drug Delivery System in Cancer,” Trends in Pharmacological Sciences42, no. 10 (2021): 857–869.

[260] S. Schuster, É. Juhász, G. Halmos, I. Neundorf, C. Gennari, and G. Mező, “Development and Biochemical Characterization of Self-Immolative Linker Containing GnRH-III-Drug Conjugates,” International Journal of Molecular Sciences23, no. 9 (2022): 5071.

[261] C. Fu, L. Yu, Y. Miao, X. Liu, Z. Yu, and M. Wei, “Peptide–Drug Conjugates (PDCs): A Novel Trend of Research and Development on Targeted Therapy, Hype or Hope?,” Acta Pharmaceutica Sinica B13, no. 2 (2023): 498–516.

[262] M. Mckean, J. Bendell, D. Petrylak, et al., “599TiP BT8009-100 Phase I/II Study of the Safety, Pharmacokinetics, & Preliminary Clinical Activity of BT8009 in Patients With Nectin-4 Expressing Advanced Malignancies,” Annals of Oncol31 (2020): S500–S501.

[263] T. Chatzisideri, G. Leonidis, T. Karampelas, et al., “Integrin-Mediated Targeted Cancer Therapy Using C (RGDyK)-Based Conjugates of Gemcitabine,” Journal of Medicinal Chemistry65, no. 1 (2021): 271–284.

[264] C. Kim, S. V. Liu, D. S. Subramaniam, et al., “Phase I Study of the177Lu-DOTA0-Tyr3-Octreotate (Lutathera) in Combination With Nivolumab in Patients With Neuroendocrine Tumors of the Lung,” Journal for Immunotherapy of Cancer8, no. 2 (2020): e000980.

[265] D. Wang, J. Liu, T. Li, et al., “A VEGFR Targeting Peptide-Drug Conjugate (PDC) Suppresses Tumor Angiogenesis in a TACE Model for Hepatocellular Carcinoma Therapy,” Cell Death Discovery8, no. 1 (2022): 411.

[266] R. Bajracharya, J. G. Song, B. R. Patil, et al., “Functional Ligands for Improving Anticancer Drug Therapy: Current Status and Applications to Drug Delivery Systems,” Drug Delivery29, no. 1 (2022): 1959–1970.

[267] J. Gong, X. Hu, J. Zhang, et al., “Phase Ia Study of CBP-1008, a Bi-Specific Ligand Drug Conjugate Targeting FRα and TRPV6, in Patients With Advanced Solid Tumors,” Journal of Clinical Oncology39 (2021): 3077.

[268] E. Ziaei, I. M. Paiva, S.-J. Yao, et al., “Peptide–Drug Conjugate Targeting Keratin 1 Inhibits Triple-Negative Breast Cancer in Mice,” Molecular Pharmaceutics20, no. 7 (2023): 3570–3577.

[269] A. Clemmensen, A. E. Hansen, P. Holst, et al., “68Ga]Ga-NODAGA-E[(cRGDyK)]2 PET and Hyperpolarized [1-13C] Pyruvate MRSI (hyperPET) in Canine Cancer Patients: Simultaneous Imaging of Angiogenesis and the Warburg Effect,” European Journal of Nuclear Medicine and Molecular Imaging48 (2021): 395–405.

[270] P. Kumthekar, S.-C. Tang, A. J. Brenner, et al., “ANG1005, a Brain-Penetrating Peptide–Drug Conjugate, Shows Activity in Patients With Breast Cancer With Leptomeningeal Carcinomatosis and Recurrent Brain Metastases,” Clinical Cancer Research26, no. 12 (2020): 2789–2799.

[271] R. A. Davis, T. Ganguly, R. Harris, S. H. Hausner, L. Kovacs, and J. L. Sutcliffe, “Synthesis and Evaluation of a Monomethyl Auristatin E-Integrin αΑ_vβ₆ Binding Peptide–Drug Conjugate for Tumor Targeted Drug Delivery,” Journal of Medicinal Chemistry66, no. 14 (2023): 9842–9852.

[272] V. P. Chavda, H. K. Solanki, M. Davidson, V. Apostolopoulos, and J. Bojarska, “Peptide-Drug Conjugates: A New Hope for Cancer Management,” Molecules27, no. 21 (2022): 7232.

[273] G. Bennett, A. Brown, G. Mudd, et al., “MMAE Delivery Using the Bicycle Toxin Conjugate BT5528,” Molecular Cancer Therapeutics19, no. 7 (2020): 1385–1394.

[274] S. Liu, Y. Tian, S. Jiang, and Z. Wang, “A Novel Homodimer Peptide–Drug Conjugate Improves the Efficacy of HER2-Positive Breast Cancer Therapy,” International Journal of Molecular Sciences24, no. 5 (2023): 4590.

[275] A. Oriol, A. Larocca, X. Leleu, et al., “Melflufen for Relapsed and Refractory Multiple Myeloma,” Expert Opinion on Investigational Drugs29, no. 10 (2020): 1069–1078.

[276] F. Schjesvold, P. Robak, L. Pour, J. Aschan, and P. Sonneveld, “OCEAN: A Randomized Phase III Study of Melflufen+ Dexamethasone to Treat Relapsed Refractory Multiple Myeloma,” Future Oncology16, no. 11 (2020): 631–641.

[277] C. T. Campbell, R. Smale, M. Rigby, et al., “Abstract 1197: A Multi Tumor Survey of Nectin-4 Expression to Guide BT8009 Indication Selection,” Cancer Research81 (2021): 1197.

[278] J. Gomena, B. Vári, R. Oláh-Szabó, et al., “Targeting the Gastrin-Releasing Peptide Receptor (GRP-R) in Cancer Therapy: Development of Bombesin-Based Peptide–Drug Conjugates,” International Journal of Molecular Sciences24, no. 4 (2023): 3400.

[279] F. Kind, K. Michalski, E. Yousefzadeh-Nowshahr, P. T. Meyer, M. Mix, and J. Ruf, “Bone Marrow Impairment During Early [¹⁷⁷Lu] PSMA-617 Radioligand Therapy: Haematotoxicity or Tumour Progression?,” EJNMMI Research12, no. 1 (2022): 20.

[280] K. Li, Y. Shi, J. Wu, et al., “An Open-Label, Non-Randomized, Multi-Center Phase I Study Evaluating the Safety, Tolerability, Pharmacokinetics and Preliminary Efficacy of Bi-Ligand-Drug Conjugate CBP-1018 in Patients With Advanced Solid Tumors,” Journal of Clinical Oncology40, no. 16 (2022): TPS2694.

[281] J. J. Sonju, A. Dahal, S. S. Singh, et al., “A pH-Sensitive Liposome Formulation of a Peptidomimetic-Dox Conjugate for Targeting HER2+ Cancer,” International Journal of Pharmaceutics612 (2022): 121364.

[282] L. Pagliaro, M. Marchesini, and G. Roti, “Targeting Oncogenic Notch Signaling With SERCA Inhibitors,” Journal of Hematology & Oncology14 (2021): 8.

[283] D. Tonnelet, M. P. Bohn, S. Becker, et al., “Angiogenesis Imaging Study Using Interim [¹⁸ F] RGD-K5 PET/CT in Patients With Lymphoma Undergoing Chemotherapy: Preliminary Evidence,” Journal of EJNMMI Research11 (2021): 1–9.

[284] J. Zhou, X. Bian, Z. Kan, et al., “In Silico Exploration and Biological Evaluation of Bispecific Peptides Derived From Anti-HER2 Antibodies and Peptide–Camptothecin Conjugates for HER2-Positive Breast Cancer,” Journal of Medicinal Chemistry65, no. 22 (2022): 15123–15139.

[285] M. Demeule, C. Charfi, J.-C. Currie, et al., “The TH1902 Docetaxel Peptide-Drug Conjugate Inhibits Xenografts Growth of Human SORT1-Positive Ovarian and Triple-Negative Breast Cancer Stem-Like Cells,” Pharmaceutics14, no. 9 (2022): 1910.

[286] Q.-Y. Zhang, Q.-L. Yu, W.-J. Luan, et al., “LWJ-M30, a Conjugate of DM1 and B6, for the Targeted Therapy of Colorectal Cancer With Improved Therapeutic Effects,” RSC Advances13, no. 16 (2023): 10840–10846.

[287] C. Gowland, P. Berry, J. Errington, et al., “Development of a LC–MS/MS Method for the Quantification of Toxic Payload DM1 Cleaved From BT1718 in a Phase I Study,” Bioanalysis13, no. 2 (2021): 101–113.

[288] X. Chen, F. Liu, X. Yu, et al., “An Auristatin-Based Peptide-Drug Conjugate Targeting Kita-Kyushu Lung Cancer Antigen 1 for Precision Chemoradiotherapy in Gastric Cancer,” European Journal of Medicinal Chemistry241 (2022): 114617.

[289] C. T. Campbell, R. Smale, J. Lee, et al., “A Survey of EphA2 Expression by Immunohistochemistry (IHC) in Tumor Tissue Microarrays (TMAs) to Support BT5528 Indication Selection,” Journal of Cancer Research80, no. 16 (2020): 5300–00.

[290] M. Demeule, C. Charfi, J. C. Currie, et al., “TH1902, a New Docetaxel-Peptide Conjugate for the Treatment of Sortilin-Positive Triple-Negative Breast Cancer,” Cancer Science112, no. 10 (2021): 4317–4334.

[291] T. Tshibangu, C. Cawthorne, K. Serdons, et al., “Automated GMP Compliant Production of [¹⁸F] AlF-NOTA-Octreotide,” EJNMMI Radiopharmacy and Chemistry5 (2020): 4.

[292] H. R. Kim, Y. S. Cho, S. W. Chung, et al., “Caspase-3 Mediated Switch Therapy of Self-Triggered and Long-Acting Prodrugs for Metastatic TNBC,” Journal of Controlled Release346 (2022): 136–147.

[293] X. Deng, R. Mai, C. Zhang, et al., “Discovery of Novel Cell-Penetrating and Tumor-Targeting Peptide-Drug Conjugate (PDC) for Programmable Delivery of Paclitaxel and Cancer Treatment,” European Journal of Medicinal Chemistry213 (2021): 113050.

[294] J. Lindberg, J. Nilvebrant, P.-Å. Nygren, and F. Lehmann, “Progress and Future Directions With Peptide-Drug Conjugates for Targeted Cancer Therapy,” Molecules26, no. 19 (2021): 6042.

[295] Y. Qi, J. Shen, C. Liu, et al., “Modularly Designed Peptide-Based Nanomedicine Inhibits Angiogenesis to Enhance Chemotherapy for Post-Surgical Recurrence of Esophageal Squamous Cell Carcinomas,” Nano Research16, no. 5 (2023): 7347–7354.

[296] A. Rocchi, T. Teesalu, and C. Celia, “Advancing Cancer-Targeted Nanotherapies With Tumor Homing Peptides,” ACS Pharmacology & Translational Science8, no. 7 (2025): 1919–1933.

[297] M. Zorko, S. Jones, and Ü. Langel, “Cell-Penetrating Peptides in Protein Mimicry and Cancer Therapeutics,” Advanced Drug Delivery Reviews180 (2022): 114044.

[298] T. Samec, J. Boulos, S. Gilmore, A. Hazelton, and A. Alexander-Bryant, “Peptide-Based Delivery of Therapeutics in Cancer Treatment,” Materials Today Bio14 (2022): 100248.

[299] C. A. Allred, C. Gormley, I. Venugopal, S. Li, M. J. McGuire, and K. C. Brown, “Tumor-Specific Intracellular Delivery: Peptide-Guided Transport of a Catalytic Toxin,” Communications Biology6, no. 1 (2023): 60.

[300] C. Alcon, M. Kovatcheva, P. Morales-Sánchez, et al., “HRK Downregulation and Augmented BCL-xL Binding to BAK Confer Apoptotic Protection to Therapy-Induced Senescent Melanoma Cells,” Cell Death & Differentiation32, no. 4 (2025): 646–656.

[301] M. R. Schnorenberg, J. A. Bellairs, R. Samaeekia, H. Acar, M. V. Tirrell, and J. L. LaBelle, “Activating the Intrinsic Pathway of Apoptosis Using Bim BH3 Peptides Delivered by Peptide Amphiphiles With Endosomal Release,” Materials12, no. 16 (2019): 2567.

[302] X. Qin, C. Fraser, A. Presser, et al., “Abstract 5731: Apoptosis Inducing Agent 1 Enhances Cancer Therapy-Induced Apoptosis by Direct Interaction With BAX and BAK,” Cancer Research83, no. 7 (2023): 5731.

[303] J. Liu, G. Shen, and X. Yan, “Bacterial Systems as a Precision Delivery Platform of Therapeutic Peptides for Cancer Therapy,” Polymer Science & Technology1, no. 6 (2025): 503–528.

[304] Y. Yang, Z. Lin, Q. Lin, W. Bei, and J. Guo, “Pathological and Therapeutic Roles of Bioactive Peptide Trefoil Factor 3 in Diverse Diseases: Recent Progress and Perspective,” Cell Death & Disease13, no. 1 (2022): 62.

[305] C. Hanisch, J. Sharbati, B. Kutz-Lohroff, O. Huber, R. Einspanier, and S. Sharbati, “Trefoil Factor 3 Mediates Resistance to Apoptosis in Colon Carcinoma Cells by a Regulatory RNA Axis,” Cell Death & Disease8, no. 3 (2017): e2660.

[306] F. P. Mesquita, F. L. de Oliveira, E. L. da Silva, et al., “Synthetic Peptides Induce Human Colorectal Cancer Cell Death via Proapoptotic Pathways,” ACS Omega9, no. 42 (2024): 43252–43263.

[307] K. Reiss, G. Yumet, S. Shan, et al., “Synthetic Peptide Sequence From the C-Terminus of the Insulin-Like Growth Factor-I Receptor That Induces Apoptosis and Inhibition of Tumor Growth,” Journal of Cellular Physiology181, no. 1 (1999): 124–135.

[308] Y. Sun, J. Li, Y. Sun, et al., “A Stable pep2-Proapoptotic Peptide Inducing Apoptosis of Acute Myeloid Leukemia Cells by Down-Regulating ezh2,” Cellular and Molecular Bioengineering13 (2020): 165–177.

[309] G. Sekar, G. Singh, X. Qin, et al., “Small Molecule SJ572946 Activates BAK to Initiate Apoptosis,” Iscience25, no. 10 (2022): 105064.

[310] K. J. Kurppa, Y. Liu, C. To, et al., “Treatment-Induced Tumor Dormancy Through YAP-Mediated Transcriptional Reprogramming of the Apoptotic Pathway,” Cancer Cell37, no. 1 (2020): 104–122.e12.

[311] K. Seidi, R. Jahanban-Esfahlan, H. Monhemi, et al., “NGR (Asn-Gly-Arg)-Targeted Delivery of Coagulase to Tumor Vasculature Arrests Cancer Cell Growth,” Oncogene37, no. 29 (2018): 3967–3980.

[312] J. Ma, X. Lian, and S. Liu, “Activating the STING Pathway to Prevent Dormant Metastasis in Lung Adenocarcinoma,” MedComm4, no. 6 (2023): e453.

[313] S.-Y. Park and J.-S. Nam, “The Force Awakens: Metastatic Dormant Cancer Cells,” Experimental & Molecular Medicine52, no. 4 (2020): 569–581.

[314] A. K. Tripathi, P. P. Desai, A. Tyagi, et al., “Short Peptides Based on the Conserved Regions of MIEN1 Protein Exhibit Anticancer Activity by Targeting the MIEN1 Signaling Pathway,” Journal of Biological Chemistry300, no. 3 (2024): 105680.

[315] Y. S. Sohn, A. Losub-Amir, A. E. Cardenas, et al., “A Peptide-Derived Strategy for Specifically Targeting the Mitochondria and ER of Cancer Cells: A New Approach in Fighting Cancer,” Chemical Science13, no. 23 (2022): 6929–6941.

[316] Z. Li, Y. Huang, T. I. Hung, et al., “MYC-Targeting Inhibitors Generated From a Stereodiversified Bicyclic Peptide Library,” Journal of the American Chemical Society146, no. 2 (2024): 1356–1363.

[317] C. P. Cerrato, M. Krkoška, Y. Sun, et al., “Engineered Peptide Coacervates Enable Efficient Intracellular Delivery of the MYC Inhibitor omoMYC,” Molecular Pharmaceutics22, no. 6 (2025): 3479–3490.

[318] P. P. Tripathi, H. Arami, I. Banga, J. Gupta, and S. Gandhi, “Cell Penetrating Peptides in Preclinical and Clinical Cancer Diagnosis and Therapy,” Oncotarget9, no. 98 (2018): 37252–37267.

[319] S. Mander, S. A. Naffouje, J. Gao, et al., “Tumor-Targeting Cell-Penetrating Peptide, p28, for Glioblastoma Imaging and Therapy,” Frontiers in Oncology12 (2022): 940001.

[320] L. Hu, J. Wang, Y. Wang, and H. Xu, “An Integrin αvβ3 Antagonistic Modified Peptide Inhibits Tumor Growth Through Inhibition of the ERK and AKT Signaling Pathways,” Oncology Reports36, no. 4 (2016): 1953–1962.

[321] Y. Song, L. Lei, X. Cai, H. Wei, and C. Y. Yu, “Immunomodulatory Peptides for Tumor Treatment,” Advanced Healthcare Materials14, no. 5 (2025): 2400512.

[322] M. Agrez, J. Rzepecka, D. Turner, et al., “A Novel Lipidic Peptide With Potential to Promote Balanced Effector-Regulatory T Cell Responses,” Scientific Reports12, no. 1 (2022): 11185.

[323] M. Agrez, C. Chandler, K. J. Thurecht, et al., “An Immunomodulating Peptide With Potential to Suppress Tumour Growth and Autoimmunity,” Scientific Reports13, no. 1 (2023): 19741.

[324] M. Mortaja, M. M. Cheng, A. Ali, et al., “Tumor-Targeted Cell-Penetrating Peptides Reveal That Monomethyl Auristatin E Temporally Modulates the Tumor Immune Microenvironment,” Molecules29, no. 23 (2024): 5618.

[325] W. Zhai, X. Zhou, M. Zhai, et al., “Blocking of the PD-1/PD-L1 Interaction by a Novel Cyclic Peptide Inhibitor for Cancer Immunotherapy,” Science China Life Sciences64 (2021): 548–562.

[326] Y. Liang, H. Luo, X. Li, et al., “PD-L1 Targeted Peptide Demonstrates Potent Antitumor and Immunomodulatory Activity in Cancer Immunotherapy,” Frontiers in Immunology15 (2024): 1367040.

[327] S. Zhong, X. Liu, T. Kaneko, et al., “Peptide Blockers of PD-1-PD-L1 Interaction Reinvigorate PD-1-Suppressed T Cells and Curb Tumor Growth in Mice,” Cells13, no. 14 (2024): 1193.

[328] P. Baldominos, A. Barbera-Mourelle, O. Barreiro, et al., “Quiescent Cancer Cells Resist T Cell Attack by Forming an Immunosuppressive Niche,” Cell185, no. 10 (2022): 1694–1708.

[329] R. Thakkar, D. Upreti, S. Ishiguro, et al., “Abstract 1352: Computational Design of a Cyclic Peptide That Inhibits the CTLA4 in T Cells and the Growth of Lung Carcinoma in Mice,” Cancer Research84, no. 6 (2024): 1352.

[330] Y. Chen, M. Li, J. Cao, et al., “CTLA-4 Promotes Lymphoma Progression Through Tumor Stem Cell Enrichment and Immunosuppression,” Open Life Sciences16, no. 1 (2021): 909–919.

[331] A. U. Kabir, M. Subramanian, D. H. Lee, et al., “Dual Role of Endothelial Myct1 in Tumor Angiogenesis and Tumor Immunity,” Science Translational Medicine13, no. 583 (2021): eabb6731.

[332] W. Zhang, M. Wang, C. Ji, X. Liu, B. Gu, and T. Dong, “Macrophage Polarization in the Tumor Microenvironment: Emerging Roles and Therapeutic Potentials,” Biomedicine & Pharmacotherapy177 (2024): 116930.

[333] J. Xu, Y. Sun, W. Fu, and S. Fu, “MYCT1 in Cancer Development: Gene Structure, Regulation, and Biological Implications for Diagnosis and Treatment,” Biomedicine & Pharmacotherapy165 (2023): 115208.

[334] Z. Wang, Y. Elbanna, I. Godet, et al., “TGF-β Induces an Atypical EMT to Evade Immune Mechanosurveillance in Lung Adenocarcinoma Dormant Metastasis,” bioRxiv84, no. 22 (2024): 618357.

[335] G. Muzes and F. Sipos, “Metastatic Cell Dormancy and Re-Activation: An Overview on Series of Molecular Events Critical for Cancer Relapse,” Anti-Cancer Agents in Medicinal Chemistry17, no. 4 (2017): 472–482.

[336] L. Zhang, X. Wang, J. Zhao, B. Sun, and W. Wang, “Construction of Targeting-Peptide-Based Imaging Reagents and Their Application in Bioimaging,” Chemical & Biomedical Imaging2, no. 4 (2023): 233–249.

[337] T. Fuchigami, T. Nakayama, Y. Miyanari, et al., “Peptide-Based Turn-on Fluorescent Probes for Highly Specific Detection of Survivin Protein in the Cancer Cells,” Chemical & Biomedical Imaging2, no. 5 (2024): 374–383.

[338] M.-Z. Cai, Z. Wen, H.-Z. Li, et al., “Peptide-Based Fluorescent Probes for the Diagnosis of Tumor and Image-Guided Surgery,” Biosensors and Bioelectronics276 (2025): 117255.

[339] Z. Sun, M. Jia, Z. Fu, M. Zhang, H. Wang, and Y. Xu, “High-Performance Disease Diagnosis Fluorescent Probe Based on New Type Structure YbF₃: Er³⁺@ SiO₂@GQDs,” Chemical Engineering Journal406 (2021): 126755.

[340] S. Naffouje, M. Goto, I. Ryoo, A. Green, T. K. Das Gupta, and T. Yamada, “A Method of Tumor In Vivo Imaging With a New Peptide-Based Fluorescent Probe,” Methods in Molecular Biology2394 (2022): 857–865.

[341] H.-W. An, D. Hou, R. Zheng, et al., “A Near-Infrared Peptide Probe With Tumor-Specific Excretion-Retarded Effect for Image-Guided Surgery of Renal Cell Carcinoma,” ACS Nano14, no. 1 (2020): 927–936.

[342] B. Hu, N. Song, Y. Cao, et al., “Noncanonical Amino Acids for Hypoxia-Responsive Peptide Self-Assembly and Fluorescence,” Journal of the American Chemical Society143, no. 34 (2021): 13854–13864.

[343] N. Laroui, N. Cubedo, M. Rossel, and N. Bettache, “Improvement of Cell Penetrating Peptide for Efficient siRNA Targeting of Tumor Xenografts in Zebrafish Embryos,” Advanced Therapeutics3, no. 2 (2020): 1900204.

[344] M. Karami Fath, K. Babakhaniyan, M. Zokaei, et al., “Anti-Cancer Peptide-Based Therapeutic Strategies in Solid Tumors,” Cellular & Molecular Biology Letters27, no. 1 (2022): 33.

[345] B. Liu, H. Zhou, L. Tan, K. T. H. Siu, and X.-Y. Guan, “Exploring Treatment Options in Cancer: Tumor Treatment Strategies,” Signal Transduction and Targeted Therapy9, no. 1 (2024): 175.

[346] A. S. Chaudhary, C. Modak, B. Gayakvad, I. Biswas, and A. Jain, “Design and Characterization of pH-Responsive DGEA-Derived Peptide Scaffolds: A Comprehensive Molecular Dynamics Simulation Study,” ACS Applied Bio Materials8, no. 3 (2025): 2459–2468.

[347] B. J. Bruno, G. D. Miller, and C. S. Lim, “Basics and Recent Advances in Peptide and Protein Drug Delivery,” Therapeutic Delivery4, no. 11 (2013): 1443–1467.

[348] X. Yang, W. Li, S. Li, et al., “Fish Oil-Based Microemulsion Can Efficiently Deliver Oral Peptide Blocking PD-1/PD-L1 and Simultaneously Induce Ferroptosis for Cancer Immunotherapy,” Journal of Controlled Release365 (2024): 654–667.

[349] X. Tan, Q. Liu, Y. Fang, et al., “Predicting Peptide Permeability Across Diverse Barriers: A Systematic Investigation,” Molecular Pharmaceutics21, no. 8 (2024): 4116–4127.

[350] M. Sugita, S. Sugiyama, T. Fujie, et al., “Large-Scale Membrane Permeability Prediction of Cyclic Peptides Crossing a Lipid Bilayer Based on Enhanced Sampling Molecular Dynamics Simulations,” Journal of Chemical Information and Modeling61, no. 7 (2021): 3681–3695.

[351] R. Wang, J. Wu, Y. Lin, et al., “An Epitope-Directed mRNA Vaccine Inhibits Tumor Metastasis Through the Blockade of MICA/B α1/2 Shedding,” Cell Reports Medicine6, no. 3 (2025): 101981.

[352] Y. Han, F. Wu, Y. Zhang, et al., “Structure-Based Design of Antibodies Targeting the EBNA1 DNA-Binding Domain to Block Epstein–Barr Virus Latent Infection and Tumor Growth,” MedComm5, no. 10 (2024): e739.

[353] S. F. A. Rizvi, S. Shahid, S. Mu, and H. Zhang, “Hybridization of Tumor Homing and Mitochondria-Targeting Peptide Domains to Design Novel Dual-Imaging Self-Assembled Peptide Nanoparticles for Theranostic Applications,” Drug. Delivery and Translational Research12, no. 5 (2021): 1285–1292.

[354] H. S. Buddhiraju, D. N. Yadav, S. Dey, K. Eswar, A. Padmakumar, and A. K. Rengan, “Advances in Peptide-Decorated Targeted Drug Delivery: Exploring Therapeutic Potential and Nanocarrier Strategies,” ACS Applied Bio Materials7, no. 8 (2023): 4879–4893.

[355] C. Liu, L. Guo, Y. Wang, J. Zhang, and C. Fu, “Delivering Metal Ions by Nanomaterials: Turning Metal Ions Into Drug-Like Cancer Theranostic Agents,” Coordination Chemistry Reviews494 (2023): 215332.

[356] M. A. Beach, U. Nayanathara, Y. Gao, et al., “Polymeric Nanoparticles for Drug Delivery,” Chemical Reviews124, no. 9 (2024): 5505–5616.

[357] C. Liu, L. Guo, Y. Cheng, et al., “A Mitochondria-Targeted Nanozyme Platform for Multi-Pathway Tumor Therapy via Ferroptosis and Cuproptosis Regulation,” Advancement of Science12, no. 36 (2025): e17616.

[358] M. J. Mitchell, M. M. Billingsley, R. M. Haley, M. E. Wechsler, N. A. Peppas, and R. Langer, “Engineering Precision Nanoparticles for Drug Delivery,” Nature Reviews Drug Discovery20, no. 2 (2021): 101–124.

[359] H. Li, P. Zhang, X. Yuan, et al., “Targeted Drug-Loaded Peptides Induce Tumor Cell Apoptosis and Immunomodulation to Increase Antitumor Efficacy,” Biomaterials Advances160 (2024): 213852.

[360] S. Peng, X. Yuan, H. Li, et al., “pH-Responsive Self-Assembling Peptides Potentiate Therapeutic Efficacy via Prolonged Drug Retention and Immunomodulation,” Materials & Design241 (2024): 112893.

[361] J. Ma, K. Kang, Y. Zhang, Q. Yi, and Z. Gu, “Detachable Polyzwitterion-Coated Ternary Nanoparticles Based on Peptide Dendritic Carbon Dots for Efficient Drug Delivery in Cancer Therapy,” ACS Applied Materials & Interfaces10, no. 50 (2018): 43923–43935.

[362] M. Sheikholeslam, S. D. Wheeler, K. G. Duke, M. Marsden, M. Pritzker, and P. Chen, “Peptide and Peptide-Carbon Nanotube Hydrogels as Scaffolds for Tissue & 3D Tumor Engineering,” Acta Biomaterialia69 (2018): 107–119.

[363] Y. Ding, Z. Sun, Z. Tong, et al., “Tumor Microenvironment-Responsive Multifunctional Peptide Coated Ultrasmall Gold Nanoparticles and Their Application in Cancer Radiotherapy,” Theranostics10, no. 12 (2020): 5195–5208.

[364] J. L. Quiles, C. Sánchez-González, L. Vera-Ramírez, et al., “Reductive Stress, Bioactive Compounds, Redox-Active Metals, and Dormant Tumor Cell Biology to Develop Redox-Based Tools for the Treatment of Cancer,” Antioxidants & Redox Signaling33, no. 12 (2020): 860–881.

[365] K. Goodarzi, R. Lane, and S. S. Rao, “Varying the RGD Concentration on a Hyaluronic Acid Hydrogel Influences Dormancy Versus Proliferation in Brain Metastatic Breast Cancer Cells,” Journal of Biomedical Materials Research. Part A112, no. 5 (2024): 710–720.

[366] Z. Xiao, K. Chen, T. Lin, P. Zhao, H. Wang, and Z. Su, “Versatile Hydrogel Drug Carrier Loading With Peptide-Carbon Dots Conjugates for Efficient Targeting and Synergistic Suppression of Breast Cancer Cell,” Materials Today Communications41 (2024): 110404.

[367] M. Elsayed, “Carbon Nanostructures as Promising Targeted Drug Delivery Systems of Anticancer Agents,” International Journal of Cancer and Biomedical Research8, no. 1 (2024): 1–15.

[368] H. Xue, J. Jin, X. Huang, et al., “Wearable Flexible Ultrasound Microneedle Patch for Cancer Immunotherapy,” Nature Communications16, no. 1 (2025): 2650.

[369] Z. Yang, H. Xu, and X. Zhao, “Designer Self-Assembling Peptide Hydrogels to Engineer 3D Cell Microenvironments for Cell Constructs Formation and Precise Oncology Remodeling in Ovarian Cancer,” Advanced Science7, no. 9 (2020): 1903718.

[370] S. Halder, T. Das, R. Kushwaha, A. K. Misra, K. Jana, and D. Das, “Targeted and Precise Drug Delivery Using a Glutathione-Responsive Ultra-Short Peptide-Based Injectable Hydrogel as a Breast Cancer Cure,” Materials Horizons12, no. 3 (2025): 987–1001.

[371] J. Mitrovic, G. Richey, S. Kim, and M. O. Guler, “Peptide Hydrogels and Nanostructures Controlling Biological Machinery,” Langmuir39, no. 34 (2023): 11935–11945.

[372] A. GhavamiNejad, J. F. Liu, S. Mirzaie, et al., “Catechol-Based Chemistry for Hypoglycemia-Responsive Delivery of Zinc-Glucagon via Hydrogel-Based Microneedle Patch Technology,” Nature Communications16, no. 1 (2025): 3124.

[373] J. Heremans, S. Ballet, and C. Martin, “The Versatility of Peptide Hydrogels: From Self-Assembly to Drug Delivery Applications,” Journal of Peptide Science31, no. 2 (2025): e3662.

[374] M. Rosa, E. Gallo, P. Pellegrino, et al., “Inclusion of Cationic Amphiphilic Peptides in Fmoc-FF Generates Multicomponent Functional Hydrogels,” ACS Applied Bio Materials8, no. 1 (2024): 488–502.

[375] Y. Xu, J. Chen, J. Ding, et al., “Synthetic Polymers for Drug, Gene, and Vaccine Delivery,” Polymer Science & Technology1, no. 3 (2025): 171–220.

[376] A. K. Moussa, H. A. Abd El-Rahman, R. R. Mohamed, and D. H. Hanna, “Hyaluronic Acid-Based pH-Sensitive Nanogel: Synthesis, Characterization, and Assessment for Acyclovir Delivery In Vitro and In Vivo,” Biomacromolecules26, no. 1 (2024): 341–362.

[377] B. Zhu, Y. Cai, L. Zhou, et al., “Injectable Supramolecular Hydrogel Co-Loading Abemaciclib/NLG919 for Neoadjuvant Immunotherapy of Triple-Negative Breast Cancer,” Nature Communications16, no. 1 (2025): 687.

[378] K. Wang, Y. Chen, S. Ahn, et al., “GD2-specific CAR T Cells Encapsulated in an Injectable Hydrogel Control Retinoblastoma and Preserve Vision,” Nature Cancer1, no. 10 (2020): 990–997.

[379] J. Kim, D. M. Francis, L. F. Sestito, et al., “Thermosensitive Hydrogel Releasing Nitric Oxide Donor and Anti-CTLA-4 Micelles for Anti-Tumor Immunotherapy,” Nature Communications13, no. 1 (2022): 1479.

[380] Y. Wang, Z. Hao, B. Li, et al., “A Novel Octa-Arginine-Modified Injectable Self-Assembling Peptide Hydrogel for Multidrug-Resistant Cancer Therapy,” Materials & Design237 (2024): 112564.

[381] X. Han, G. Li, S. You, et al., “Injectable Bio-Multifunctional Hyaluronic Acid-Based Hydrogels Loaded With Poly ADP-Ribose Polymerase Inhibitors for Ovarian Cancer Therapy,” International Journal of Biological Macromolecules270 (2024): 132275.

[382] D. T. Nguyen, L. H. Dang, H. K. Le, et al., “Injectable Hyaluronic Acid–Cyclodextrin-Based Hydrogels for Localized and Sustained Release of Anticancer Drugs,” Macromolecular Research32, no. 8 (2024): 777–788.

[383] L.-H. Chen, N.-W. Liang, W.-Y. Huang, et al., “Supramolecular Hydrogel for Programmable Delivery of Therapeutics to Cancer Multidrug Resistance,” Biomaterials Advances146 (2023): 213282.

[384] Q. Luo, Z. Gao, J. Liu, et al., “Bioactive Peptide-Based Electroactive Hydrogels for Myocardial Infarction Treatment via Electrical and Microenvironmental Regulation,” ACS Applied Materials & Interfaces17, no. 22 (2025): 32066–32080.

[385] M. Cherri, P. S. Stergiou, Z. Ahmadian, et al., “Redox-Responsive Hydrogels Loaded With an Antibacterial Peptide as Controlled Drug Delivery for Healing Infectious Wounds,” Advanced Healthcare Materials13, no. 27 (2024): 2401289.

[386] X. Bao, X. Si, X. Ding, L. Duan, and C. Xiao, “pH-Responsive Hydrogels Based on the Self-Assembly of Short Polypeptides for Controlled Release of Peptide and Protein Drugs,” Journal of Polymer Research26 (2019): 278.

[387] Y. Yu, Y. Zhao, Y. Zou, et al., “Ultra-Sensitive pH Responsive Hydrogels With Injectable and Self-Healing Performance for Controlled Drug Delivery,” International Journal of Pharmaceutics: X9 (2025): 100334.

[388] G. Ye, S. Luo, H. Zafar, et al., “pH-Sensitive Supramolecular Self-Assembled Peptide Hydrogel for the Treatment of Esophageal Cancer,” Frontiers in Pharmacology15 (2024): 1453422.

[389] Z. Dai, Q. Zhang, X. Li, et al., “In Situ Forming pH/ROS-Responsive Niche-Like Hydrogel for Ultrasound-Mediated Multiple Therapy in Synergy With Potentiating Anti-Tumor Immunity,” Materials Today65 (2023): 62–77.

[390] C. J. Farino Reyes and J. H. Slater, “Tuning Hydrogel Adhesivity and Degradability to Model the Influence of Premetastatic Niche Matrix Properties on Breast Cancer Dormancy and Reactivation,” Advanced Biology6, no. 5 (2022): 2200012.

[391] K. Goodarzi and S. S. Rao, “Structurally Decoupled Hyaluronic Acid Hydrogels for Studying Matrix Metalloproteinase-Mediated Invasion of Metastatic Breast Cancer Cells,” International Journal of Biological Macromolecules277 (2024): 134493.

[392] R. V. Kondapaneni, L. A. Shevde, and S. S. Rao, “A Biomimetic Hyaluronic Acid Hydrogel Models Mass Dormancy in Brain Metastatic Breast Cancer Spheroids,” Advanced Biology7, no. 1 (2023): 2200114.

[393] Y. Zhao, J. Qin, D. Yu, et al., “Polymer-Locking Fusogenic Liposomes for Glioblastoma-Targeted siRNA Delivery and CRISPR–Cas Gene Editing,” Nature Nanotechnology19 (2024): 1869–1879.

[394] Q. T. H. Shubhra, “Multi-Compartment Liposomes Forge New Paths in Drug Delivery,” Nature Chemistry16, no. 10 (2024): 1578–1579.

[395] L. Jiang, S. Zhou, X. Zhang, et al., “Mitochondrion-Specific Dendritic Lipopeptide Liposomes for Targeted Sub-Cellular Delivery,” Nature Communications12, no. 1 (2021): 2390.

[396] N. Meng, J. Lu, J. Zhou, et al., “Improved Immunocompatibility of Active Targeting Liposomes by Attenuating Nucleophilic Attack of Cyclic RGD Peptides on Complement 3,” Biomaterials321 (2025): 123350.

[397] Z. Song, Y. Lin, X. Zhang, et al., “Cyclic RGD Peptide-Modified Liposomal Drug Delivery System for Targeted Oral Apatinib Administration: Enhanced Cellular Uptake and Improved Therapeutic Effects,” International Journal of Nanomedicine12 (2017): 1941–1958.

[398] J. J. Sonju, A. Dahal, S. S. Singh, and S. D. Jois, “Peptide-Functionalized Liposomes as Therapeutic and Diagnostic Tools for Cancer Treatment,” Journal of Controlled Release329 (2021): 624–644.

[399] E. Yuba, M. Takashima, T. Hayashi, et al., “Multifunctional Traceable Liposomes With Temperature-Triggered Drug Release and Neovasculature-Targeting Properties for Improved Cancer Chemotherapy,” Molecular Pharmaceutics18, no. 9 (2021): 3342–3351.

[400] E. Khabazian, F. Vakhshiteh, P. Norouzi, Y. Fatahi, R. Dinarvand, and F. Atyabi, “Cationic Liposome Decorated With Cyclic RGD Peptide for Targeted Delivery of anti-STAT3 siRNA to Melanoma Cancer Cells,” Journal of Drug Targeting30, no. 5 (2022): 522–533.

[401] L. Yin, X. Li, R. Wang, Y. Zeng, Z. Zeng, and T. Xie, “Recent Research Progress of RGD Peptide–Modified Nanodrug Delivery Systems in Tumor Therapy,” International Journal of Peptide Research and Therapeutics29, no. 4 (2023): 53.

[402] M. Amin, T. Lammers, and T. L. M. Ten Hagen, “Temperature-Sensitive Polymers to Promote Heat-Triggered Drug Release From Liposomes: Towards Bypassing EPR,” Advanced Drug Delivery Reviews189 (2022): 114503.

[403] Y. Lee and D. H. Thompson, “Stimuli-Responsive Liposomes for Drug Delivery,” WIREs Nanomedicine and Nanobiotechnology9, no. 5 (2017): e1450.

[404] J. Lee, J. Byun, G. Shim, and Y.-K. Oh, “Fibroblast Activation Protein Activated Antifibrotic Peptide Delivery Attenuates Fibrosis in Mouse Models of Liver Fibrosis,” Nature Communications13, no. 1 (2022): 1516.

[405] D. K. Arya, P. Pandey, A. Kumar, et al., “Dual-Ligand Functionalized Liposomes With iRGD/Trastuzumab Co-Loaded With Gefitinib and Lycorine for Enhanced Metastatic Breast Cancer Therapy,” Journal of Liposome Research35, no. 2 (2025): 173–187.

[406] Y. Cai, X. Zhang, W. Hu, et al., “Enhancing Transdermal Delivery of Chrysomycin A for the Treatment of Cutaneous Melanoma and MRSA Infections Using Skin-Penetrating Peptide-Functionalized Deformable Liposomes,” International Journal of Pharmaceutics670 (2025): 125130.

[407] Y. Liu, Y. Xie, Y. Chen, et al., “A Protease-Cleavable Liposome for Co-Delivery of Anti-PD-L1 and Doxorubicin for Colon Cancer Therapy in Mice,” Nature Communications16, no. 1 (2025): 2854.

[408] M.-A. Jourdain and J. Eyer, “Recent Advances in Liposomes and Peptide-Based Therapeutics for Glioblastoma Treatment,” Journal of Controlled Release376 (2024): 732–752.

[409] H. Han, J.-H. Jung, H. Lee, et al., “Targeted Fusogenic Liposomes for Effective Tumor Delivery and Penetration of Lipophilic Cargoes,” ACS Biomaterials Science & Engineering9, no. 4 (2023): 1919–1927.

[410] H. Y. Kim, M. Kang, Y. W. Choo, et al., “Immunomodulatory Lipocomplex Functionalized With Photosensitizer-Embedded Cancer Cell Membrane Inhibits Tumor Growth and Metastasis,” Nano Letters19, no. 8 (2019): 5185–5193.

[411] K. Zhang, X. Fang, Q. You, et al., “Novel Peptide-Directed Liposomes for Targeted Combination Therapy of Breast Tumors,” Materials Advances1, no. 9 (2020): 3483–3495.

[412] J. G. Altin and Y. Zhao, “Using Peptides to Promote Delivery and Improve Anti-Tumour Efficacy of Liposomal Drug,” Journal of Drug Targeting30, no. 5 (2022): 544–556.

[413] J. Ma, L. Fang, Z. Sun, et al., “Folate-PEG-PROTAC Micelles for Enhancing Tumor-Specific Targeting Proteolysis In Vivo,” Advanced Healthcare Materials13, no. 20 (2024): 2400109.

[414] K. Manna, A. Roy, S. Dey, S. Ghosh, P. Pradhan, and S. Pal, “A Review on the Culmination of Rational Development of Stimuli-Responsive Polymeric Micelles as Vehicles for Site-Specific Hydrophobic Therapeutics,” Journal of Macromolecular Science, Part A61, no. 6 (2024): 349–375.

[415] R. Salah Othman, S. Zarei, H. Rezaei Haghighat, A. Afshar Taromi, and H. A. Khonakdar, “Recent Advances in Smart Polymeric Micelles for Targeted Drug Delivery,” Polymers for Advanced Technologies36, no. 4 (2025): e70180.

[416] M. Ghezzi, S. Pescina, C. Padula, et al., “Polymeric Micelles in Drug Delivery: An Insight of the Techniques for Their Characterization and Assessment in Biorelevant Conditions,” Journal of Controlled Release332 (2021): 312–336.

[417] I. Ahmad, P. Kushwaha, S. Usmani, and A. Tiwari, “Polymeric Micelles: Revolutionizing Cancer Therapeutics for Enhanced Efficacy,” BioNanoScience15, no. 1 (2025): 186.

[418] Y. Yuan, W. Tan, Y. Mi, L. Wang, Z. Qi, and Z. Guo, “Effect of Hydrophobic Chain Length in Amphiphilic Chitosan Conjugates on Intracellular Drug Delivery and Smart Drug Release of Redox-Responsive Micelle,” Marine Drugs22, no. 1 (2023): 18.

[419] X. Wang, M. Zhang, Y. Li, H. Cong, B. Yu, and Y. Shen, “Research Status of Dendrimer Micelles in Tumor Therapy for Drug Delivery,” Small19, no. 50 (2023): 2304006.

[420] W. Y. Fu, Y.-L. Chiu, S.-C. Huang, et al., “Boron Neutron Capture Therapy Enhanced by Boronate Ester Polymer Micelles: Synthesis, Stability, and Tumor Inhibition Studies,” Biomacromolecules25, no. 7 (2024): 4215–4232.

[421] Y. Lu and K. Park, “Polymeric Micelles and Alternative Nanonized Delivery Vehicles for Poorly Soluble Drugs,” International Journal of Pharmaceutics453, no. 1 (2013): 198–214.

[422] B. Ghosh and S. Biswas, “Polymeric Micelles in Cancer Therapy: State of the Art,” Journal of Controlled Release332 (2021): 127–147.

[423] A. S. Deshmukh, P. N. Chauhan, M. N. Noolvi, et al., “Polymeric Micelles: Basic Research to Clinical Practice,” International Journal of Pharmaceutics532, no. 1 (2017): 249–268.

[424] Y. Cai, Z. Xu, Q. Shuai, et al., “Tumor-Targeting Peptide Functionalized PEG-PLA Micelles for Efficient Drug Delivery,” Biomaterials Science8, no. 8 (2020): 2274–2282.

[425] W. Fan, J. Xiang, Q. Wei, et al., “Role of Micelle Size in Cell Transcytosis-Based Tumor Extravasation, Infiltration, and Treatment Efficacy,” Nano Letters23, no. 9 (2023): 3904–3912.

[426] Z. Lu, K. Yan, C. Liu, J. Wang, G. Yu, and H. Zhang, “Novel pH-Sensitive Triptolide-Loaded Micelles: A Potential Approach to Increase Anti-Tumor Activity of the Diterpenoid Epoxide,” Journal of Nanoparticle Research26, no. 4 (2024): 68.

[427] Z. Han, Z. Li, R. Raveendran, et al., “Peptide-Conjugated Micelles Make Effective Mimics of the TRAIL Protein for Driving Apoptosis in Colon Cancer,” Biomacromolecules24, no. 11 (2023): 5046–5057.

[428] K. Yan, Y. Feng, K. Gao, X. Shi, and X. Zhao, “Fabrication of Hyaluronic Acid-Based Micelles With Glutathione-Responsiveness for Targeted Anticancer Drug Delivery,” Journal of Colloid and Interface Science606 (2022): 1586–1596.

[429] J. Bai, J. Wang, Y. Feng, Y. Yao, and X. Zhao, “Stability-Tunable Core-Crosslinked Polymeric Micelles Based on an Imidazole-Bearing Block Polymer for pH-Responsive Drug Delivery,” Colloids and Surfaces, A: Physicochemical and Engineering Aspects639 (2022): 128353.

[430] Y. Wang, M. Lin, T. Fan, M. Zhou, R. Yin, and X. Wang, “Advances of Stimuli-Responsive Amphiphilic Copolymer Micelles in Tumor Therapy,” International Journal of Nanomedicine20 (2024): 1–24.

[431] Z. Su, Z. Xiao, Y. Wang, et al., “Codelivery of Anti-PD-1 Antibody and Paclitaxel With Matrix Metalloproteinase and pH Dual-Sensitive Micelles for Enhanced Tumor Chemoimmunotherapy,” Small16, no. 7 (2020): 1906832.

[432] Y. Zhuo, Z. Luo, Z. Zhu, et al., “Direct Cytosolic Delivery of siRNA via Cell Membrane Fusion Using Cholesterol-Enriched Exosomes,” Nature Nanotechnology19, no. 12 (2024): 1858–1868.

[433] Q. Zhan, K. Yi, X. Li, et al., “Phosphatidylcholine-Engineered Exosomes for Enhanced Tumor Cell Uptake and Intracellular Antitumor Drug Delivery,” Macromolecular Bioscience21, no. 8 (2021): 2100042.

[434] M. S. Kishta, A. Khamis, H. Am, A. H. Elshaar, and D. Gül, “Exploring the Tumor-Suppressive Role of miRNA-200c in Head and Neck Squamous Cell Carcinoma: Potential and Mechanisms of Exosome-Mediated Delivery for Therapeutic Applications,” Translational Oncology51 (2025): 102216.

[435] M. A. Kumar, S. K. Baba, H. Q. Sadida, et al., “Extracellular Vesicles as Tools and Targets in Therapy for Diseases,” Signal Transduction and Targeted Therapy9, no. 1 (2024): 27.

[436] X. Chen, Y. Li, M. Li, et al., “Exosomal miRNAs Assist in the Crosstalk Between Tumor Cells and Immune Cells and Its Potential Therapeutics,” Life Sciences329 (2023): 121934.

[437] S. G. Gabaran, N. Ghasemzadeh, M. Rahnama, E. Karatas, A. Akbari, and J. Rezaie, “Functionalized Exosomes for Targeted Therapy in Cancer and Regenerative Medicine: Genetic, Chemical, and Physical Modifications,” Cell Communication and Signaling23, no. 1 (2025): 265.

[438] J. Zhou, X. Cheng, Z. Guo, et al., “Epitope Imprinting of Phospholipids by Oriented Assembly at the Oil/Water Interface for the Selective Recognition of Plasma Membranes,” Angewandte Chemie135, no. 19 (2023): e202213938.

[439] X. Meng, J. Wang, J. Zhou, et al., “Tumor Cell Membrane-Based Peptide Delivery System Targeting the Tumor Microenvironment for Cancer Immunotherapy and Diagnosis,” Acta Biomaterialia127 (2021): 266–275.

[440] N. H. Tran, D. D. Nguyen, N. M. Nguyen, et al., “Dual-Targeting Exosomes for Improved Drug Delivery in Breast Cancer,” Nanomedicine18, no. 7 (2023): 599–611.

[441] M. Li, S. Li, C. Du, et al., “Exosomes From Different Cells: Characteristics, Modifications, and Therapeutic Applications,” European Journal of Medicinal Chemistry207 (2020): 112784.

[442] M. Basak, D. K. Chaudhary, R. Takahashi, et al., “Immunocyte Derived Exosomes: Insight Into the Potential Chemo-Immunotherapeutic Nanocarrier Targeting the Tumor Microenvironment,” ACS Biomaterials Science & Engineering9, no. 1 (2022): 20–39.

[443] G. Zhang, S. Cen, X. Huang, et al., “Size Matters: Curvature and Antigen-Mediated Dual Recognition of Size-Specific Tumor-Derived Exosomes,” Analytical Chemistry96, no. 44 (2024): 17897–17906.

[444] Y. Zhao, T. Liu, and M. Zhou, “Immune-Cell-Derived Exosomes for Cancer Therapy,” Molecular Pharmaceutics19, no. 9 (2022): 3042–3056.

[445] Q. Liu, G. Dai, Y. Wu, et al., “iRGD-Modified Exosomes-Delivered BCL6 siRNA Inhibit the Progression of Diffuse Large B-Cell Lymphoma,” Frontiers in Oncology12 (2022): 822805.

[446] M. Yang, X. Wang, F. Pu, et al., “Engineered Exosomes-Based Photothermal Therapy With MRI/CT Imaging Guidance Enhances Anticancer Efficacy Through Deep Tumor Nucleus Penetration,” Pharmaceutics13, no. 10 (2021): 1593.

[447] B. Tao, R. Du, X. Zhang, et al., “Engineering CAR-NK Cell Derived Exosome Disguised Nano-Bombs for Enhanced HER2 Positive Breast Cancer Brain Metastasis Therapy,” Journal of Controlled Release363 (2023): 692–706.

[448] H. Xu, C. Liao, S. Liang, and B.-C. Ye, “A Novel Peptide-Equipped Exosomes Platform for Delivery of Antisense Oligonucleotides,” ACS Applied Materials & Interfaces13, no. 9 (2021): 10760–10767.

[449] X. Chu, D. Li, X. Fang, et al., “Immunochemotherapeutic Nanoparticles Inhibit Cancer-Promoting Fibroblasts Subtypes for Pancreatic Ductal Adenocarcinoma,” Nano Today62 (2025): 102709.

[450] G. R. Gunassekaran, S. M. Poongkavithai Vadevoo, M.-C. Baek, and B. Lee, “M1 Macrophage Exosomes Engineered to Foster M1 Polarization and Target the IL-4 Receptor Inhibit Tumor Growth by Reprogramming Tumor-Associated Macrophages Into M1-like Macrophages,” Biomaterials278 (2021): 121137.

[451] H. Cheng, J.-H. Fan, L.-P. Zhao, et al., “Chimeric Peptide Engineered Exosomes for Dual-Stage Light Guided Plasma Membrane and Nucleus Targeted Photodynamic Therapy,” Biomaterials211 (2019): 14–24.

[452] W. Chen, Y. Mao, Y. Zhan, et al., “Exosome-Delivered NR2F1-AS1 and NR2F1 Drive Phenotypic Transition From Dormancy to Proliferation in Treatment-Resistant Prostate Cancer via Stabilizing Hormonal Receptors,” Journal of Nanobiotechnology22, no. 1 (2024): 761.

[453] R. Bhatia, J. Chang, J. L. Munoz, and N. D. Walker, “Forging New Therapeutic Targets: Efforts of Tumor Derived Exosomes to Prepare the Pre-Metastatic Niche for Cancer Cell Dissemination and Dormancy,” Biomedicines11, no. 6 (2023): 1614.

[454] B. Dai, A. M. Clark, and A. Wells, “Mesenchymal Stem Cell-Secreted Exosomes and Soluble Signals Regulate Breast Cancer Metastatic Dormancy: Current Progress and Future Outlook,” International Journal of Molecular Sciences25, no. 13 (2024): 7133.

[455] S. A. Bliss, G. Sinha, O. A. Sandiford, et al., “Mesenchymal Stem Cell–Derived Exosomes Stimulate Cycling Quiescence and Early Breast Cancer Dormancy in Bone Marrow,” Cancer Research76, no. 19 (2016): 5832–5844.

[456] L. Xu, Q. Liu, H. Liu, et al., “Disrupting CCDC137-Mediated LZTS2 and β-TrCP Interaction in the Nucleus Inhibits Hepatocellular Carcinoma Development via β-Catenin and AKT,” Cell Death and Differentiation32, no. 1 (2024): 134–148.

[457] J. L. Warthen and M. J. Lueckheide, “Peptides as Targeting Agents and Therapeutics: A Brief Overview,” Biomacromolecules25, no. 11 (2024): 6923–6935.

[458] S. M. P. Vadevoo, S. Gurung, H.-S. Lee, et al., “Peptides as Multifunctional Players in Cancer Therapy,” Experimental & Molecular Medicine55, no. 6 (2023): 1099–1109.

[459] V. Balayan and A. K. Guddati, “Tumor Dormancy: Biologic and Therapeutic Implications,” World Journal of Oncology13, no. 1 (2022): 8–19.

[460] S. Bonet Olivencia and F. Sasangohar, “Investigating the Food and Drug Administration Biotherapeutics Review and Approval Process: Narrative Review,” JMIR Formative Research5, no. 3 (2021): e14563.

[461] Z. Han, D. Feng, W. Wang, et al., “Influence of Fatty Acid Modification on the Anticancer Activity of the Antimicrobial Peptide Figainin 1,” ACS Omega8, no. 44 (2023): 41876–41884.

[462] G. Dong, L. Gong, Q. Zhang, et al., “Glycosylation Modification Balances the Aqueous Solubility of Lipidated Peptides and Facilitates Their Biostability,” Bioconjugate Chemistry36, no. 5 (2025): 1004–1012.

[463] Y. Liu, D. H. T. Le, G. Yilmaz, et al., “Targeted Peptide Nanofiber-Loaded Stomatocytes for Combined Photodynamic and Photothermal Therapy,” ACS Applied Materials & Interfaces17, no. 24 (2025): 35230–35239.

[464] K. Sharma, K. K. Sharma, A. Sharma, and R. Jain, “Peptide-Based Drug Discovery: Current Status and Recent Advances,” Drug Discovery Today28, no. 2 (2023): 103464.

[465] T. Saric, C. I. Graef, and A. L. Goldberg, “Pathway for Degradation of Peptides Generated by Proteasomes,” Journal of Biological Chemistry279, no. 45 (2004): 46723–46732.

[466] C. S. Brian Chia, “A Review on the Metabolism of 25 Peptide Drugs,” International Journal of Peptide Research and Therapeutics27, no. 2 (2021): 1397–1418.

[467] P. Pei, R. Wei, B. Wang, J. Su, Z. Zhang, and W. Liu, “An Advanced Tunable Multimodal Luminescent La₄GeO₈: Eu²⁺, Er³⁺ Phosphor for Multicolor Anticounterfeiting,” Advanced Functional Materials31, no. 31 (2021): 2102479.

[468] H. Chen, Y. Dong, F. Shi, and F. Li, “Engineering the Bioactive Profile of Medicinal Peptides by Multiarm Polyethylene Glycol Conjugation,” Langmuir41, no. 15 (2025): 9932–9940.

[469] N. Abbasi Gharibkandi, J. M. Conlon, and S. J. Hosseinimehr, “Strategies for Improving Stability and Pharmacokinetic Characteristics of Radiolabeled Peptides for Imaging and Therapy,” Peptides133 (2020): 170385.

[470] L. Diao and B. Meibohm, “Pharmacokinetics and Pharmacokinetic–Pharmacodynamic Correlations of Therapeutic Peptides,” Clinical Pharmacokinetics52 (2013): 855–868.

[471] H. Guo and Y. Miao, “Cu-64-Labeled Lactam Bridge-Cyclized α-MSH Peptides for PET Imaging of Melanoma,” Molecular Pharmaceutics9, no. 8 (2012): 2322–2330.

[472] L. Xu, X. Fan, Y. He, X. Xia, and J. Zhang, “Design, Synthesis, and Biological Evaluation of Lysine-Stapled Peptide Inhibitors of p53-MDM2/MDMX Interactions With Potent Antitumor Activity In Vivo,” Journal of Medicinal Chemistry67, no. 19 (2024): 17893–17904.

[473] H. Li, X. Chen, M. Wu, P. Song, and X. Zhao, “Bicyclic Stapled Peptides Based on p53 as Dual Inhibitors for the Interactions of p53 With MDM2 and MDMX,” Chinese Chemical Letters33, no. 3 (2022): 1254–1258.

[474] Y. Guo, X. Chu, Y. Deng, et al., “Development of a Novel Ultra-Acidic Self-Assembling Peptides-Based Hydrogel System for pH-Tunable Nanobody Delivery,” Advanced Materials Technologies10, no. 8 (2025): 2401581.

[475] A. W. Du and M. H. Stenzel, “Drug Carriers for the Delivery of Therapeutic Peptides,” Biomacromolecules15, no. 4 (2014): 1097–1114.

[476] M. Singh, G. Kaur, and I. Singh, “Molecular Self-Assembly of Peptides Into Supramolecular Nanoarchitectures for Target-Specific Drug Delivery,” ACS Applied Bio Materials8, no. 6 (2025): 4467–4488.

[477] D. Ran, J. Mao, C. Zhan, et al., “D-Retroenantiomer of Quorum-Sensing Peptide-Modified Polymeric Micelles for Brain Tumor-Targeted Drug Delivery,” ACS Applied Materials & Interfaces9, no. 31 (2017): 25672–25682.

[478] X. L. Wu, J. H. Kim, H. Koo, et al., “Tumor-Targeting Peptide Conjugated pH-Responsive Micelles as a Potential Drug Carrier for Cancer Therapy,” Bioconjugate Chemistry21, no. 2 (2010): 208–213.

[479] A. Recasens and L. Munoz, “Targeting Cancer Cell Dormancy,” Trends in Pharmacological Sciences40, no. 2 (2019): 128–141.

[480] B. D. Khalil, R. Sanchez, T. Rahman, et al., “An NR2F1-Specific Agonist Suppresses Metastasis by Inducing Cancer Cell Dormancy,” Journal of Experimetnal Medicine219, no. 1 (2021): e20210836.

[481] D. Kumar, G. Bansal, A. Narang, T. Basak, T. Abbas, and D. Dash, “Integrating Transcriptome and Proteome Profiling: Strategies and Applications,” Proteomics16, no. 19 (2016): 2533–2544.

[482] P. Iglesias, C. Penas, L. Barral-Cagiao, E. Pazos, and J. A. Costoya, “A Bio-Inspired Hypoxia Sensor Using HIF1a-oxygen-dependent Degradation Domain,” Scientific Reports9, no. 1 (2019): 7117.

[483] J. Wang, J. Liu, and Z. Yang, “Recent Advances in Peptide-Based Nanomaterials for Targeting Hypoxia,” Nanoscale Advances3, no. 21 (2021): 6027–6039.

[484] E. Ashrafichoobdar, T. Perez, L. Ayalew, V. Gorbanwand, J. Monroy, and K. Slowinska, “Hybrid Peptides as Platform for Synchronized Combination Therapy,” Colloids and Surfaces B: Biointerfaces226 (2023): 113326.

[485] N. Mehrotra, S. Kharbanda, and H. Singh, “Peptide-Based Combination Nanoformulations for Cancer Therapy,” Nanomedicine15, no. 22 (2020): 2201–2217.

[486] H.-Y. Min and H.-Y. Lee, “Cellular Dormancy in Cancer: Mechanisms and Potential Targeting Strategies,” Cancer Research and Treatment55, no. 3 (2023): 720–736.

[487] A. J. Stephens, N. A. Burgess-Brown, and S. Jiang, “Beyond Just Peptide Antigens: The Complex World of Peptide‑Based Cancer Vaccines,” Frontiers in immunology12 (2021): Front. Immunol.): 696791.

[488] J.-W. Kim, T.-D. Kim, B. S. Hong, et al., “A Serum-Stable Branched Dimeric Anti-VEGF Peptide Blocks Tumor Growth via Anti-Angiogenic Activity,” Experimental and Molecular Medicine42, no. 7 (2010): 514–523.

[489] J. A. Marin-Acevedo, B. Dholaria, A. E. Soyano, K. L. Knutson, S. Chumsri, and Y. Lou, “Next Generation of Immune Checkpoint Therapy in Cancer: New Developments and Challenges,” Journal of Hematology & Oncology11 (2018): 39.

[490] Z. Zhao, J. Fetse, U.-F. Mamani, et al., “Development of a Peptide-Based Tumor-Activated Checkpoint Inhibitor for Cancer Immunotherapy,” Acta Biomaterialia193 (2025): 484–497.

[491] B. A. Shah, J. A. Holden, J. C. Lenzo, S. Hadjigol, and N. M. O'Brien-Simpson, “Multi-Disciplinary Approaches Paving the Way for Clinically Effective Peptide Vaccines for Cancer,” NPJ Vaccines10, no. 1 (2025): 68.

[492] Y. Du, Y. Liu, D. Wang, et al., “Peptidic Microarchitecture-Trapped Tumor Vaccine Combined With Immune Checkpoint Inhibitor or PI3Kγ Inhibitor Can Enhance Immunogenicity and Eradicate Tumors,” Journal for Immunotherapy of Cancer10, no. 2 (2022): e003564.

[493] Y. Cai, M. Gong, M. Zeng, et al., “Immunopeptidomics-Guided Discovery and Characterization of Neoantigens for Personalized Cancer Immunotherapy,” Science Advances11, no. 21 (2025): eadv6445.

[494] L. Buonaguro and M. Tagliamonte, “Peptide-Based Vaccine for Cancer Therapies,” Frontiers in Immunology14 (2023): 1210044.

[495] L. Ferrazzano, M. Catani, A. Cavazzini, et al., “Sustainability in Peptide Chemistry: Current Synthesis and Purification Technologies and Future Challenges,” Green Chemistry24, no. 3 (2022): 975–1020.

[496] A. Isidro-Llobet, M. N. Kenworthy, S. Mukherjee, et al., “Sustainability Challenges in Peptide Synthesis and Purification: From R&D to Production,” Journal of Organic Chemistry84, no. 8 (2019): 4615–4628.

[497] D. Zane, P. L. Feldman, T. Sawyer, Z. Sobol, and J. Hawes, “Development and Regulatory Challenges for Peptide Therapeutics,” International Journal of Toxicology40 (2021): 108–124.

[498] V. Sanna and M. Sechi, “Therapeutic Potential of Targeted Nanoparticles and Perspective on Nanotherapies,” ACS Medicinal Chemistry Letters11, no. 6 (2020): 1069–1073.

[499] Y. Yang, L. Hansen, and J.-M. Receveur, “Quality Management of Diastereomeric Impurity for Complex Peptide Manufacturing: A Case Study of Corticorelin Ovine,” Organic Process Research & Development29, no. 6 (2025): 1617–1624.

[500] X. Luo, H. Chen, Y. Song, et al., “Advancements, Challenges and Future Perspectives on Peptide-Based Drugs: Focus on Antimicrobial Peptides,” European Journal of Pharmaceutical Sciences181 (2023): 106363.

[501] A. J. Pereira, L. J. de Campos, H. Xing, and M. Conda-Sheridan, “Peptide-Based Therapeutics: Challenges and Solutions,” Medicinal Chemistry Research33, no. 8 (2024): 1275–1280.

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2025 The Author(s). MedComm – Oncology published by John Wiley & Sons Australia, Ltd on behalf of Sichuan International Medical Exchange & Promotion Association (SCIMEA).