CNRS, Université de Paris, UPR 9080, Laboratoire de Biochimie Théorique, Paris, France; Institut de Biologie Physico-Chimique-Fondation Edmond de Rothschild, PSL Research University, Paris, France.
Laboratory of Theoretical Chemistry, Ton Duc Thang University, Ho Chi Minh City, Vietnam; Faculty of Pharmacy, Ton Duc Thang University, Ho Chi Minh City, Vietnam.
Prog Mol Biol Transl Sci. 2020;170:435-460. doi: 10.1016/bs.pmbts.2019.12.002. Epub 2020 Jan 6.
Protein misfolding and aggregation of amyloid proteins is the fundamental cause of more than 20 diseases. Molecular mechanisms of the self-assembly and the formation of the toxic aggregates are still elusive. Computer simulations have been intensively used to study the aggregation of amyloid peptides of various amino acid lengths related to neurodegenerative diseases. We review atomistic and coarse-grained simulations of short amyloid peptides aimed at determining their transient oligomeric structures and the early and late aggregation steps.
蛋白质错误折叠和淀粉样蛋白的聚集是 20 多种疾病的根本原因。淀粉样蛋白的自组装和有毒聚集体的形成的分子机制仍然难以捉摸。计算机模拟已被广泛用于研究与神经退行性疾病相关的各种氨基酸长度的淀粉样肽的聚集。我们综述了短淀粉样肽的原子和粗粒模拟，旨在确定它们的瞬态寡聚结构以及早期和晚期的聚集步骤。
