1. Academic Validation
  2. Formation of β-Lactoglobulin Self-Assemblies via Liquid-Liquid Phase Separation for Applications beyond the Biological Functions

Formation of β-Lactoglobulin Self-Assemblies via Liquid-Liquid Phase Separation for Applications beyond the Biological Functions

  • ACS Appl Mater Interfaces. 2021 Oct 6;13(39):46391-46405. doi: 10.1021/acsami.1c14634.
Tuo-Di Zhang 1 Xudong Deng 1 Meng-Ying Wang 2 Liang-Liang Chen 1 Xue-Ting Wang 1 Chen-Yuan Li 1 Wen-Pu Shi 1 Wen-Juan Lin 1 Qiang Li 3 Weichun Pan 4 Xiaodan Ni 5 Tiezheng Pan 1 Da-Chuan Yin 1
Affiliations

Affiliations

  • 1 School of Life Sciences, Northwestern Polytechnical University, Xi'an 710072, Shaanxi, People's Republic of China.
  • 2 Laboratory for Structural Biology of Infection and Inflammation, Institute of Biochemistry and Molecular Biology, c/o DESY, Building 22a, Notkestr. 85, Hamburg 22607, Germany.
  • 3 School of Materials Science and Engineering, Northwestern Polytechnical University, Xi'an 710072, Shaanxi, People's Republic of China.
  • 4 Food Safety Key Lab of Zhejiang Province, The School of Food Science and Biotechnology, Zhejiang Gongshang University, Hangzhou 310018, People's Republic of China.
  • 5 Laboratory of Membrane Proteins and Structural Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892, United States.
Abstract

Proteins are like miracle machines, playing important roles in living organisms. They perform vital biofunctions by further combining together and/or with other biomacromolecules to form assemblies or condensates such as membraneless organelles. Therefore, studying the self-assembly of biomacromolecules is of fundamental importance. In addition to their biological activities, protein assemblies also exhibit extra properties that enable them to achieve applications beyond their original functions. Herein, this study showed that in the presence of Monosaccharides, ethylene glycols, and Amino acids, β-lactoglobulin (β-LG) can form assemblies with specific structures, which were highly reproducible. The mechanism of the assembly process was studied through multi-scale observations and theoretical analysis, and it was found that the assembling all started from the formation of solute-rich liquid droplets via liquid-liquid phase separation (LLPS). These droplets then combined together to form condensates with elaborate structures, and the condensates finally evolved to form assemblies with various morphologies. Such a mechanism of the assembly is valuable for studying the assembly processes that frequently occur in living organisms. Detailed studies concerning the properties and applications of the obtained β-LG assemblies showed that the assemblies exhibited significantly better performances than the protein itself in terms of autofluorescence, antioxidant activity, and metal ion absorption, which indicates broad applications of these assemblies in bioimaging, biodetection, biodiagnosis, health maintenance, and pollution treatment. This study revealed that biomacromolecules, especially proteins, can be assembled via LLPS, and some unexpected application potentials could be found beyond their original biological functions.

Keywords

antioxidant activity; autofluorescence; bioimaging; biomolecules; metal ion absorption; β-lactoglobulin self-assemblies.

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