Molecular modeling, simulation and docking study of ebola virus glycoprotein
Molecular modeling, simulation and docking study of ebola virus glycoprotein
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DOI：
10.1016/j.jmgm.2016.12.010
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发表时间：
2017-03-01
影响因子：
2.9
通讯作者：
Khan, Khalid
中科院分区：
文献类型：
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作者：
Ahmad, Nasir;Farman, Aqsa;Khan, Khalid
埃博拉病毒（EBOV）是一种丝状、包膜、无节段、负链核糖核酸（RNA）病毒，属于丝状病毒科。埃博拉病毒包括不同的糖蛋白，每种糖蛋白在病毒生命周期的不同方面发挥作用。本研究从Uniprot获得埃博拉病毒分泌糖蛋白（Q7T9E0）。通过在线服务器预测了二级结构α -螺旋和β -薄片的形成。通过RONN， GLOBPLOT和DISSEMBLE检测蛋白质的高柔韧性和无序区域。通过同源建模技术和MOE软件构建蛋白的三维结构。通过RAMPAGE和ERRAT服务器两种立体化学测试确定了改进模型的有效性和评价。通过MOE对给定蛋白与两种抗病毒药物drone - edarone和胺碘酮的不同衍生物进行进一步对接研究。对接评分和各自衍生物的结合亲和力表明它们可能用作蛋白质受体。(C) 2016 Elsevier Inc.版权所有。
Ebola virus (EBOV) is a filamentous, enveloped, non-segmented, negative-strand ribonucleic acid (RNA) virus which belongs to family Filoviridae. Ebola virus includes different glycoproteins each of which plays their roles in different aspects of viral life cycle. In this study secreted glycoprotein (Q7T9E0) of Ebola virus was acquired from Uniprot. The formation of alpha helix and beta sheets of secondary structures were predicted through online servers. Higher flexibility and disordered regions of proteins were determined through RONN, GLOBPLOT and DISSEMBLE. Three dimensional (3D) structure of the protein was built through homology modeling techniques and MOE software. The validation and evaluation of the refined models were determined with two stereochemical tests i-e RAMPAGE and ERRAT servers. Further docking studies of given protein was performed with different derivatives of two antiviral drugs dronedarone and amiodarone through MOE. Docking score and binding affinity of respective derivatives demonstrate that these might be used as protein receptors. (C) 2016 Elsevier Inc. All rights reserved.