Recent progress on understanding the mechanisms of amyloid nucleation

被引：120

作者：

Chatani E. ^{[1
]}

Yamamoto N. ^{[1
]}

机构：

[1] Graduate School of Science, Kobe University, 1-1 Rokkodai, Nada, Kobe, 657-8501, Hyogo

来源：

Biophysical Reviews | 2018年 / 10卷 / 2期

基金：

日本学术振兴会;

关键词：

Amyloid fibril; Nucleated conformational conversion; Nucleation; Oligomer; Precursor;

D O I：

10.1007/s12551-017-0353-8

中图分类号：

学科分类号：

摘要：

Amyloid fibrils are supramolecular protein assemblies with a fibrous morphology and cross-β structure. The formation of amyloid fibrils typically follows a nucleation-dependent polymerization mechanism, in which a one-step nucleation scheme has widely been accepted. However, a variety of oligomers have been identified in early stages of fibrillation, and a nucleated conformational conversion (NCC) mechanism, in which oligomers serve as a precursor of amyloid nucleation and convert to amyloid nuclei, has been proposed. This development has raised the need to consider more complicated multi-step nucleation processes in addition to the simplest one-step process, and evidence for the direct involvement of oligomers as nucleation precursors has been obtained both experimentally and theoretically. Interestingly, the NCC mechanism has some analogy with the two-step nucleation mechanism proposed for inorganic and organic crystals and protein crystals, although a more dramatic conformational conversion of proteins should be considered in amyloid nucleation. Clarifying the properties of the nucleation precursors of amyloid fibrils in detail, in comparison with those of crystals, will allow a better understanding of the nucleation of amyloid fibrils and pave the way to develop techniques to regulate it. © 2017, International Union for Pure and Applied Biophysics (IUPAB) and Springer-Verlag GmbH Germany, part of Springer Nature.

引用

页码：527 / 534

页数：7

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