多巴胺
尼古丁
黑质
α-突触核蛋白
化学
分子动力学
帕金森病
机制(生物学)
神经科学
生物物理学
立体化学
生物
物理
医学
疾病
计算化学
内科学
多巴胺能
量子力学
出处
期刊:Journal of computational biophysics and chemistry
[World Scientific]
日期:2021-07-07
卷期号:20 (05): 477-494
标识
DOI:10.1142/s2737416521500265
摘要
Parkinson’s disease (PD) is a progressive nervous system disorder and its pathological hallmark is the presence of fibrillar aggregates called Lewy bodies (LB) in substantia nigra. As it is also well established, [Formula: see text]-synuclein is the major constituent of the LB. Although numerous experimental studies have been conducted on inhibition of [Formula: see text]-synuclein aggregation, the detailed inhibitory mechanism is not still fully elucidated. In this paper, we first focused on identifying the binding modes of nicotine and dopamine to [Formula: see text]-synuclein using molecular docking. Then, we performed comparative molecular dynamics (MD) simulations to enlighten the inhibition mechanism of [Formula: see text]-synuclein for both dopamine and nicotine. MD simulations demonstrate that both nicotine and dopamine stabilize dominant helical structure of [Formula: see text]-synuclein and so they inhibit their conformational transitions. Moreover, the favorable and unfavorable contribution residues, which play a key role in the inhibition of [Formula: see text]-synuclein, were determined using MM-PBSA analysis. The findings in this study will shed light on understanding the inhibition mechanism of [Formula: see text]-synuclein and guide potential drug development studies of degenerative diseases.
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