Publication:
Molecular docking studies of chromone derivatives against wild type and mutant strains of HIV-1 protease

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Issued Date

2014

Resource Type

Article

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application/pdf

ISSN

10542523

DOI

10.1007/s00044-014-0992-2

Other identifier(s)

2-s2.0-84896434812

Rights Holder(s)

Scopus

Bibliographic Citation

Medicinal Chemistry Research. Vol 23, No.9 (2014), p.4198-4208

Suggested Citation

Nunthanavanit P., Ungwitayatorn J. Molecular docking studies of chromone derivatives against wild type and mutant strains of HIV-1 protease. Medicinal Chemistry Research. Vol 23, No.9 (2014), p.4198-4208. doi:10.1007/s00044-014-0992-2 Retrieved from: https://hdl.handle.net/20.500.14740/6503

Title

Molecular docking studies of chromone derivatives against wild type and mutant strains of HIV-1 protease

Author(s)

Nunthanavanit P.
 Ungwitayatorn J.

Abstract

Developing a new HIV-1 protease (HIV-1 PR) inhibitor is still a challenging task to overcome the drug resistance mutations in the HIV-PR. In this study, docking simulations of chromone derivatives against wild type and eleven mutant variants HIV-1 PR were investigated using GOLD and Autodock programs. From both GOLD and Autodock results, chromone 3, the experimentally observed highly potent HIV-1 PR inhibitor, showed stronger binding affinity against every studied mutant strain (2AVS, 2AVO, 2AVV, 1MES, 1MET, 1MEU, 1SDU, 1SDV, 1C6Y, 2F8O, and 1SH9) than the wild-type enzyme (1AJX). Chromone 32, another potent inhibitor as well as chromones 33, 34, 37, and 47 also showed high binding interaction with several mutant-type enzymes. The coherent picture of the interactions at the active sites of mutant PR should facilitate the further design and development of new potent inhibitor against multidrug-resistant virus. © 2014 Springer Science+Business Media New York.

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https://hdl.handle.net/20.500.14740/6503

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Scopus: Year 1983-2021

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