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

Formation of beta-Lactoglobulin Self-Assemblies via Liquid-Liquid Phase Separation for Applications beyond the Biological Functions
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通过液-液相分离形成 β-乳球蛋白自组装体,用于超越生物功能的应用

DOI:
10.1021/acsami.1c14634
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发表时间:
2021
影响因子:
9.5
通讯作者:
Yin Da-Chuan
Yin Da-Chuan
中科院分区:
材料科学2区
文献类型:
--
作者:
Zhang Tuo-Di;Deng Xudong;Wang Meng-Ying;Chen Liang-Liang;Wang Xue-Ting;Li Chen-Yuan;Shi Wen-Pu;Lin Wen-Juan;Li Qiang;Pan Weichun;Ni Xiaodan;Pan Tiezheng;Yin Da-Chuan

文献摘要

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蛋白质就像是神奇的机器,在生物体中扮演着重要的角色。它们通过进一步结合在一起和/或与其他生物大分子结合以形成组装体或凝聚物如无膜细胞器来执行重要的生物功能。因此,研究生物大分子的自组装具有十分重要的意义。除了它们的生物活性,蛋白质组装体还表现出额外的性质,使它们能够实现超出其原始功能的应用。在此,本研究表明,在单糖,乙二醇和氨基酸的存在下,β-乳球蛋白(β-LG)可以形成具有特定结构的组装体,这是高度可重复的。通过多尺度观测和理论分析研究了组装过程的机理,发现组装过程均始于液-液相分离(LLPS)形成富含溶质的液滴。然后这些液滴结合在一起形成具有精细结构的冷凝物,并且冷凝物最终演化形成具有各种形态的组装体。这种组装机制对于研究生物体中经常发生的组装过程是有价值的。对所获得的β-LG组装体的性质和应用进行了详细的研究,结果表明,组装体在自发荧光、抗氧化活性和金属离子吸附等方面均明显优于蛋白本身,在生物成像、生物检测、生物诊断、健康维护和污染治理等方面具有广泛的应用前景。研究表明,生物大分子,特别是蛋白质,可以通过LLPS组装,并发现了一些意想不到的应用潜力超出其原有的生物功能。
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.