Molecular docking and simulation of Zika virus NS3 helicase

BMC Chemistry

Ashfaq Ur Rehman¹  Asad Ullah²  Syed Lal Badshah²  Nasir Ahmad²  Khalid Khan²  Yahia N. Mabkhot³  Abdulrhman Alsayari⁴  Abdullatif Bin Muhsinah⁴ 

[1]0000 0004 0368 8293, grid.16821.3c, State Key Laboratory of Microbial Metabolism, Department of Bioinformatics and Biostatistics, Shanghai Jiao Tong University, 800 Dongchuan Road, 200240, Shanghai, China

[2]0000 0004 0496 8545, grid.459615.a, Department of Chemistry, Islamia College University, Peshawar, Khyber Pakhtunkhwa, Pakistan

[3]0000 0004 1790 7100, grid.412144.6, Department of Pharmaceutical Chemistry, College of Pharamacy, King Khalid University, 61441, Abha, Saudi Arabia

[4]0000 0004 1790 7100, grid.412144.6, Department of Pharmacognosy, College of Pharmacy, King Khalid University, 62529, Abha, Saudi Arabia

关键词: ZIKV;    Microcephaly;    Nonstructural protein-3 Helicase;    Molecular dynamics simulation;    Molecular docking;   

DOI  :  10.1186/s13065-019-0582-y

来源: publisher

【 摘 要 】

The Zika virus (ZIKV) has gained attention for the last few years due to the congenital microcephaly and Guillain–Barre Syndrome that resulted in humans. The non-structural protein-3 (NS3) helicase of ZIKV play an important role in viral RNA replication. In this article, we performed hundred nanosecond molecular dynamics simulation and molecular docking of the NS3 helicase of ZIKV with 1,4-benzothiazine derivatives. The root mean square deviation (RMSD) analyses showed the stability of the NS3 helicase. The simulation showed that the flexible and rigid domains of the protein play a crucial role during the RNA replication process. All such domains with ligand binding pockets can be targeted for drug design. The molecular docking showed that the strong hydrogen bonding and arene-cation interactions are responsible for the binding between NS3 and 1,4-benzothiazine derivatives, which provides a new dimension for potent drug design for ZIKV.

【 授权许可】

CC BY