Frontiers of Chemical Science and Engineering >
Effect of ligand chain length on hydrophobic charge induction chromatography revealed by molecular dynamics simulations
Received date: 02 Aug 2013
Accepted date: 21 Sep 2013
Published date: 05 Dec 2013
Copyright
Hydrophobic charge induction chromatography (HCIC) is a mixed-mode chromatography which is advantageous for high adsorption capacity and facile elution. The effect of the ligand chain length on protein behavior in HCIC was studied. A coarse-grain adsorbent pore model established in an earlier work was modified to construct adsorbents with different chain lengths, including one with shorter ligands (CL2) and one with longer ligands (CL4). The adsorption, desorption, and conformational transition of the proteins with CL2 and CL4 were examined using molecular dynamics simulations. The ligand chain length has a significant effect on both the probability and the irreversibility of the adsorption/desorption. Longer ligands reduced the energy barrier of adsorption, leading to stronger and more irreversible adsorption, as well as a little more unfolding of the protein. The simulation results elucidated the effect of the ligand chain length, which is beneficial for the rational design of adsorbents and parameter optimization for high-performance HCIC.
Lin ZHANG , Yan SUN . Effect of ligand chain length on hydrophobic charge induction chromatography revealed by molecular dynamics simulations[J]. Frontiers of Chemical Science and Engineering, 2013 , 7(4) : 456 -463 . DOI: 10.1007/s11705-013-1357-y
1 |
Burton S C, Harding D R. Hydrophobic charge induction chromatography: Salt independent protein adsorption and facile elution with aqueous buffers. Journal of Chromatography. A, 1998, 814(1-2): 71-81
|
2 |
Schwartz W, Judd D, Wysocki M, Guerrier L, Birck-Wilson E, Boschetti E. Comparison of hydrophobic charge induction chromatography with affinity chromatography on protein A for harvest and purification of antibodies. Journal of Chromatography. A, 2001, 908(1-2): 251-263
|
3 |
Dux M P, Barent R, Sinha J, Gouthro M, Swanson T, Barthuli A, Inan M, Ross J T, Smith L A, Smith T J, Webb R, Loveless B, Henderson I, Meagher M M. Purification and scale-up of a recombinant heavy chain fragment C of botulinum neurotoxin serotype E in Pichia pastoris GS115. Protein Expression and Purification, 2006, 45(2): 359-367
|
4 |
Weatherly G T, Bouvier A, Lydiard D D, Chapline J, Henderson I, Schrimsher J L, Shepard S R. Initial purification of recombinant botulinum neurotoxin fragments for pharmaceutical production using hydrophobic charge induction chromatography. Journal of Chromatography. A, 2002, 952(1-2): 99-110
|
5 |
Guerrier L, Girot P, Schwartz W, Boschetti E. New method for the selective capture of antibodies under physiolgical conditions. Bioseparation, 2000, 9(4): 211-221
|
6 |
Guerrier L, Flayeux I, Boschetti E. A dual-mode approach to the selective separation of antibodies and their fragments. Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences, 2001, 755(1-2): 37-46
|
7 |
Boschetti E. Antibody separation by hydrophobic charge induction chromatography. Trends in Biotechnology, 2002, 20(8): 333-337
|
8 |
Zhao G F, Sun Y. Displacement chromatography of proteins on hydrophobic charge induction adsorbent column. Journal of Chromatography. A, 2007, 1165(1-2): 109-115
|
9 |
Ghose S, Hubbard B, Cramer S M. Evaluation and comparison of alternatives to Protein A chromatography —Mimetic and hydrophobic charge induction chromatographic stationary phases. Journal of Chromatography. A, 2006, 1122(1-2): 144-152
|
10 |
Coulon D, Cabanne C, Fitton V, Noubhani A M, Saint-Christophe E, Santarelli X. Penicillin acylase purification with the aid of hydrophobic charge induction chromatography. Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences, 2004, 808(1): 111-115
|
11 |
Zhao G F, Peng G Y, Li F Q, Shi Q H, Sun Y. 5-Aminoindole, a new ligand for hydrophobic charge induction chromatography. Journal of Chromatography. A, 2008, 1211(1-2): 90-98
|
12 |
Lin D, Tong H, Wang H, Shao S, Yao S. Molecular mechanism of hydrophobic charge-induction chromatography: Interactions between the immobilized 4-mercaptoethyl-pyridine ligand and IgG. Journal of Chromatography. A, 2012, 1260: 143-153
|
13 |
Tong H, Lin D, Gao D, Yuan X, Yao S. Caprylate as the albumin-selective modifier to improve IgG purification with hydrophobic charge-induction chromatography. Journal of Chromatography. A, 2013, 1285: 88-96
|
14 |
Lu H, Lin D, Gao D, Yao S. Evaluation of immunoglobulin adsorption on the hydrophobic charge-induction resins with different ligand densities and pore sizes. Journal of Chromatography. A, 2013, 1278: 61-68
|
15 |
Lippa K A, Sander L C. Identification of isolated cavity features within molecular dynamics simulated chromatographic surfaces. Journal of Chromatography. A, 2006, 1128(1-2): 79-89
|
16 |
Sander L C, Lippa K A, Wise S A. Order and disorder in alkyl stationary phases. Analytical and Bioanalytical Chemistry, 2005, 382(3): 646-668
|
17 |
Lippa K A, Sander L C, Mountain R D. Molecular dynamics Simulations of alkylsilane stationary-phase order and disorder. 2. Effects of temperature and chain length. Analytical Chemistry, 2005, 77(24): 7862-7871
|
18 |
Rafferty J L, Siepmann J I, Schure M R. The effects of chain length, embedded polar groups, pressure, and pore shape on structure and retention in reversed-phase liquid chromatography: Molecular-level insights from Monte Carlo simulations. Journal of Chromatography. A, 2009, 1216(12): 2320-2331
|
19 |
Braun J, Fouqueau A, Bemish R J, Meuwly M. Solvent structures of mixed water/acetonitrile mixtures at chromatographic interfaces from computer simulations. Physical Chemistry Chemical Physics, 2008, 10(32): 4765-4777
|
20 |
Fouqueau A, Meuwly M, Bemish R J. Adsorption of acridine orange at a C-8,C-18/Water/Acetonitrile interface. Journal of Physical Chemistry B, 2007, 111(34): 10208-10216
|
21 |
Gritti F, Guiochon G. A chromatographic estimate of the degree of surface heterogeneity of reversed-phase liquid chromatography packing materials II-Endcapped monomeric C-18-bonded stationary phase. Journal of Chromatography. A, 2006, 1103(1): 57-68
|
22 |
Singh S, Wegmann J, Albert K, Muller K. Variable temperature FT-IR studies of n-alkyl modified silica gels. Journal of Physical Chemistry B, 2002, 106(4): 878-888
|
23 |
Tan L C, Carr P W. Revisionist look at solvophobic driving forces in reversed-phase liquid chromatography: II. Partitioning vs adsorption mechanism in monomeric alkyl bonded phase supports. Journal of Chromatography. A, 1997, 775(1-2): 1-12
|
24 |
Hennion M C, Picard C, Caude M. Influence of the number and length of alkyl chains on the chromatographic properteis of hyrdrocarbonaceous bonded phases. Journal of Chromatography. A, 1978, 166(1): 21-35
|
25 |
Miyabe K, Guiochon G. Influence of the modification conditions of alkyl bonded ligands on the characteristics of reversed-phase liquid chromatography. Journal of Chromatography. A, 2000, 903(1-2): 1-12
|
26 |
Lienqueo M E, Mahn A, Salgado J C, Asenjo J A. Current insights on protein behaviour in hydrophobic interaction chromatography. Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences, 2007, 849(1-2): 53-68
|
27 |
Er-el Z, Zaidenzaig Y, Shaltiel S. Hydrocarbon-coated Sepharoses. Use in the purification of glycogen phosphorylase. Biochemical and Biophysical Research Communications, 1972, 49(2): 383-390
|
28 |
Dias-Cabral A C, Ferreira A S, Phillips J, Queiroz J A, Pinto N G. The effects of ligand chain length, salt concentration and temperature on the adsorption of bovine serum albumin onto polypropyleneglycol-Sepharose. Biomedical Chromatography, 2005, 19(8): 606-616
|
29 |
Lin F Y, Chen W Y, Ruaan R C, Huang H M. Microcalorimetric studies of interactions between proteins and hydrophobic ligands in hydrophobic interaction chromatography: Effects of ligand chain length, density and the amount of bound protein. Journal of Chromatography. A, 2000, 872(1-2): 37-47
|
30 |
Busini V, Moiani D, Moscatelli D, Zamolo L, Cavallotti C. Investigation of the influence of spacer arm on the structural evolution of affinity ligands supported on agarose. Journal of Physical Chemistry B, 2006, 110(46): 23564-23577
|
31 |
Salvalaglio M, Cavallotti C. Molecular modeling to rationalize ligand-support interactions in affinity chromatography. Journal of Separation Science, 2012, 35(1): 7-19
|
32 |
Zhang L, Zhao G F, Sun Y. Molecular insight into protein conformational transition in hydrophobic charge induction chromatography: A molecular dynamics simulation. Journal of Physical Chemistry B, 2009, 113(19): 6873-6880
|
33 |
Zhang L, Zhao G F, Sun Y. Effects of ligand density on hydrophobic charge induction chromatography: Molecular dynamics simulation. Journal of Physical Chemistry B, 2010, 114(6): 2203-2211
|
34 |
Zhang L, Bai S, Sun Y. Molecular dynamics simulation of the effect of ligand homogeneity on protein behavior in hydrophobic charge induction chromatography. Journal of Molecular Graphics & Modelling, 2010, 28(8): 863-869
|
35 |
Zhang L, Zhao G F, Sun Y. Molecular dynamics simulation and experimental validation of the effect of pH on protein desorption in hydrophobic charge induction chromatography. Molecular Simulation, 2010, 36(13): 1096-1103
|
36 |
Zhao G F, Zhang L, Bai S, Sun Y. Analysis of hydrophobic charge induction displacement chromatography by visualization with confocal laser scanning microscopy. Separation and Purification Technology, 2011, 82: 138-147
|
37 |
Honeycutt J D, Thirumalai D. Metastability of the folded states of globular proteins. Proceedings of the National Academy of Sciences of the United States of America, 1990, 87(9): 3526-3529
|
38 |
Berendsen H J, Vanderspoel D, Vandrunen R. Gromacs—A message-passing parallel molecular-dynamics implementation. Computer Physics Communications, 1995, 91(1-3): 43-56
|
39 |
Lindahl E, Hess B. van S D. GROMACS 3.0: A package for molecular simulation and trajectory analysis. Journal of Molecular Modeling, 2001, 7(8): 306-317
|
40 |
Sayle R, Milnerwhite E. RASMOL—Biomolecular graphics for all. Trends in Biochemical Sciences, 1995, 20(9): 374-376
|
/
〈 | 〉 |