Author:
Huang Kai-Fang,Dong Shu-Heng,Zhong Su-Su,Li Hao,Duan Li-Li
Abstract
Abstract
One major cause of Alzheimer’s disease (AD) is evidently due to the aggregation and deposition of amyloid β peptides (Aβ) in the brain tissue of the patient. Preventing misfolding and self-aggregation of Aβ protein can reduce the formation of highly toxic polymer, which is important for the treatment of AD. Among them, the α-helix consisting of 42 residues (Aβ42) is the main component of senile plaques in AD. In this paper, 500 ns accelerated molecular dynamics are performed at different temperatures (300 K, 350 K, 400 K, 450 K) to study of the effect of temperature-induced conformation changes of Aβ42 protein during the unfolding process respectively.
Subject
Physics and Astronomy (miscellaneous)
Cited by
5 articles.
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