Xia Kui, Shen Haolei, Wang Peng, Tan Rongri, Xun Damao
Department of Physics, Jiangxi Science and Technology Normal University, Nanchang, China.
J Biomol Struct Dyn. 2023 Jul-Aug;41(12):5872-5881. doi: 10.1080/07391102.2022.2099466. Epub 2022 Jul 15.
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.
当蛋白质的构象从天然状态转变为错误折叠状态时，会引发一些疾病，如朊病毒病。朊病毒病是一组由朊病毒蛋白错误折叠和聚集引起的致命神经退行性疾病。一元醇对蛋白质结构有很大影响。然而，一元醇是否能抑制淀粉样纤维化仍不确定。在此，为阐明乙醇对人朊病毒蛋白结构稳定性的影响，采用分子动力学模拟分析了不同温度下人朊病毒蛋白的构象变化和动力学特征。结果表明，在高温下，β-折叠的延伸更容易发生，α-螺旋更容易被破坏。我们发现乙醇可以破坏疏水相互作用并使氢键稳定，从而保护蛋白质的二级结构，尤其是在500K时。由拉马斯瓦米·H·萨尔马传达。
