Formation of β-Lactoglobulin Self-Assemblies via Liquid-Liquid Phase Separation for Applications beyond the Biological Functions
| Autor: | Qiang Li, Meng-Ying Wang, Chen-Yuan Li, Wen-Pu Shi, Tuo-Di Zhang, Da-Chuan Yin, Xue-Ting Wang, Tiezheng Pan, Weichun Pan, Liang-Liang Chen, Xudong Deng, Wen-Juan Lin, Xiaodan Ni |
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| Rok vydání: | 2021 |
| Předmět: |
chemistry.chemical_classification
Materials science Biomolecule Iron Nanotechnology Hydrogen Bonding Lactoglobulins Molecular Dynamics Simulation Antioxidants Molecular Docking Simulation chemistry.chemical_compound Mice RAW 264.7 Cells chemistry Lead Liquid liquid Health maintenance Animals General Materials Science Absorption (chemistry) Protein Multimerization Ethylene glycol Copper Chelating Agents Protein Binding |
| Zdroj: | ACS applied materialsinterfaces. 13(39) |
| ISSN: | 1944-8252 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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