Interaction between amylose, fatty acid, and β-lactoglobulin to study multiple biomacromolecules self-assembly and application

Aggregate ›› 2024, Vol. 5 ›› Issue (4) : e536

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Aggregate ›› 2024, Vol. 5 ›› Issue (4) : e536 DOI: 10.1002/agt2.536
RESEARCH ARTICLE

Interaction between amylose, fatty acid, and β-lactoglobulin to study multiple biomacromolecules self-assembly and application

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Abstract

New concept for the development of supramolecular assemblies from intricate interactions between different classes of biomacromolecules (polysaccharides, proteins and lipids) is yet to come, due to their intrinsic chemical and structural complexity and incompatibility. Herein, we report an interaction mechanism among multiple biomacromolecules, and the structural and digestive properties of their assemblies using amylose (AM), lauric acid (LA), and β-lactoglobulin (βLG) as exemplars. AM, LA, and βLG interact to form a water-soluble ternary complex through van der Waals forces between AM and LA and high affinity binding between AM and βLG, which can further assemble into uniform-sized, semi-crystalline nanospheres under certain thermodynamic conditions. These nanospheres are substantially resistant to amylolysis, thus can be well utilized by gut microbiota, including increasing short-chain fatty acid levels and shaping bacterial communities. Illustrating the complexation of AM, LA, and βLG and their assemblies from disorder to order, this work offers potential rationale of assemblies for multiple biomacromolecules driven by non-covalent interactions and substantial potentials for supramolecular biomaterials development.

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amylose-lipid-protein complex / biomacromolecules / gut microbiota / multicomponent interaction / polymeric nanospheres / supramolecular self-assembly

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null. Interaction between amylose, fatty acid, and β-lactoglobulin to study multiple biomacromolecules self-assembly and application. Aggregate, 2024, 5(4): e536 DOI:10.1002/agt2.536

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