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Cu 结合 S100B 会引发二硫键交联四聚体的聚合，从而增强对淀粉样β聚集的分子伴侣活性。

Cu-binding to S100B triggers polymerization of disulfide cross-linked tetramers with enhanced chaperone activity against amyloid-β aggregation.

机构信息

Biosystems and Integrative Sciences Institute, Faculdade de Ciências, Universidade de Lisboa, Lisboa 1749-016, Portugal.

出版信息

Chem Commun (Camb). 2021 Jan 14;57(3):379-382. doi: 10.1039/d0cc06842j.

DOI:10.1039/d0cc06842j
PMID:33326534
Abstract

S100B is an extracellular protein implicated in Alzheimer's Disease and a suppressor of amyloid-β aggregation. Herein we report a mechanism tying Cu2+ binding to a change in assembly state yielding disulfide cross-linked oligomers with higher anti-aggregation activity. This chemical control of chaperone function illustrates a regulatory process relevant under metal and proteostasis dysfunction as in neurodegeneration.

摘要

S100B 是一种细胞外蛋白，与阿尔茨海默病有关，并且是淀粉样β聚集的抑制剂。本文报道了一种将 Cu2+ 结合与组装状态变化联系起来的机制，产生具有更高抗聚集活性的二硫键交联低聚物。这种伴侣蛋白功能的化学控制说明了在金属和蛋白质稳态功能障碍（如神经退行性变）下相关的调节过程。

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