Ahmad Nasir, Farman Aqsa, Badshah Syed Lal, Ur Rahman Ata, Ur Rashid Haroon, Khan Khalid
Department of Chemistry, Islamia College University, Peshawar, Khyber Pakhtunkhwa, Pakistan.
Institute of Chemical Sciences, University of Peshawar, Peshawar, Khyber Pakhtunkhwa, Pakistan.
J Mol Graph Model. 2017 Mar;72:266-271. doi: 10.1016/j.jmgm.2016.12.010. Epub 2016 Dec 19.
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.
埃博拉病毒（EBOV）是一种丝状、包膜、不分节段的负链核糖核酸（RNA）病毒，属于丝状病毒科。埃博拉病毒包含不同的糖蛋白，每种糖蛋白在病毒生命周期的不同方面发挥作用。在本研究中，埃博拉病毒的分泌型糖蛋白（Q7T9E0）取自通用蛋白质数据库（Uniprot）。通过在线服务器预测二级结构的α螺旋和β折叠的形成。通过RONN、GLOBPLOT和DISSEMBLE确定蛋白质的更高灵活性和无序区域。通过同源建模技术和分子操作环境（MOE）软件构建蛋白质的三维（3D）结构。使用两个立体化学测试即RAMPAGE和ERRAT服务器确定优化模型的验证和评估。通过MOE对两种抗病毒药物决奈达隆和胺碘酮的不同衍生物与给定蛋白质进行进一步的对接研究。各自衍生物的对接分数和结合亲和力表明这些可能用作蛋白质受体。
