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由无规卷曲区域介导的蜘蛛丝蛋白的纳米组装。

Nanoassembly of spider silk protein mediated by intrinsically disordered regions.

机构信息

Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, Singapore 117543, Singapore.

Department of Chemistry, University of British Columbia, Vancouver, BC V6T 1Z1, Canada.

出版信息

Int J Biol Macromol. 2024 Jun;271(Pt 1):132438. doi: 10.1016/j.ijbiomac.2024.132438. Epub 2024 May 16.

Abstract

Spider silk is the self-assembling product of silk proteins each containing multiple repeating units. Each repeating unit is entirely intrinsically disordered or contains a small disordered domain. The role of the disordered domain/unit in conferring silk protein storage and self-assembly is not fully understood yet. Here, we used biophysical and biochemical techniques to investigate the self-assembly of a miniature version of a minor ampullate spidroin (denoted as miniMiSp). miniMiSp consists of two identical intrinsically disordered domains, one folded repetitive domain, and two folded terminal domains. Our data indicated that miniMiSp self-assembles into oligomers and further into liquid droplets. The oligomerization is attributed to the aggregation-prone property of both the disordered domains and the folded repetitive domain. Our results support the model of micellar structure for silk proteins at high protein concentrations. The disordered domain is indispensable for liquid droplet formation via liquid-liquid phase separation, and tyrosine residues located in the disordered domain make dominant contributions to stability of the liquid droplets. As the same tyrosine residues are also critical to fibrillation, the liquid droplets are likely an intermediate state between the solution state and the fiber state. Additionally, the terminal domains contribute to the pH- and salt-dependent self-assembly properties.

摘要

蜘蛛丝是由含有多个重复单元的丝蛋白自组装而成的产物。每个重复单元完全是无规的,或者含有一个小的无规结构域。无规结构域/单元在赋予丝蛋白储存和自组装能力方面的作用尚未完全了解。在这里,我们使用生物物理和生化技术研究了一种小型的小型壶腹丝蛋白(表示为 miniMiSp)的自组装。miniMiSp 由两个相同的无规结构域、一个折叠重复结构域和两个折叠末端结构域组成。我们的数据表明,miniMiSp 自组装成低聚物,然后进一步自组装成液滴。低聚物的形成归因于无规结构域和折叠重复结构域的聚集倾向特性。我们的结果支持了高浓度蛋白质下丝蛋白胶束结构的模型。无规结构域对于通过液-液相分离形成液滴是必不可少的,位于无规结构域中的酪氨酸残基对液滴的稳定性有很大贡献。由于相同的酪氨酸残基对纤维化也很关键,因此液滴可能是溶液状态和纤维状态之间的中间状态。此外,末端结构域有助于 pH 值和盐依赖性自组装特性。

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