分子动力学
化学
蛋白质折叠
氢键
蛋白质聚集
朊蛋白
生物物理学
蛋白质结构
淀粉样蛋白(真菌学)
乙醇
淀粉样纤维
生物化学
淀粉样β
生物
分子
计算化学
疾病
有机化学
医学
无机化学
病理
作者
Kui Xia,Haolei Shen,Peng Wang,Rongri Tan,Da-Mao Xun
标识
DOI:10.1080/07391102.2022.2099466
摘要
When the conformation of protein is changed from its natural state to a misfolded state, some diseases will happen like prion disease. Prion diseases are a set of deadly neurodegenerative diseases caused by prion protein misfolding and aggregation. Monohydric alcohols have a strong influence on the structure of protein. However, whether monohydric alcohols inhibit amyloid fibrosis remains uncertain. Here, to elucidate the effect of ethanol on the structural stability of human prion protein, molecular dynamics simulations were employed to analyze the conformational changes and dynamics characteristics of human prion proteins at different temperatures. The results show that the extension of β-sheet occurs more easily and the α-helix is more easily disrupted at high temperatures. We found that ethanol can destroy the hydrophobic interactions and make the hydrogen bonds stable, which protects the secondary structure of the protein, especially at 500 K.Communicated by Ramaswamy H. Sarma.
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