Discovery of Mycobacterium tuberculosis CYP121 new inhibitor via structure-based drug repurposing

Tuberculosis (TB) remains a serious threat to human health with the advent of multi-drug resistant tuberculosis (MDR-TB) and extensively drug-resistant tuberculosis (XDR-TB). The urge to find novel drugs to deal with the appearance of drug-resistant TB and its variants is highly needed. This study a...

Full description

Bibliographic Details
Main Authors: El Moudaka, Tarek, Murugan, Priya, Abdul Rahman, Mohd Basyaruddin, Tejo, Bimo Ario
Format: Article
Language:English
Published: Universiti Putra Malaysia Press 2022
Online Access:http://psasir.upm.edu.my/id/eprint/100974/
http://psasir.upm.edu.my/id/eprint/100974/1/Discovery%20of%20Mycobacterium%20tuberculosis%20.pdf
_version_ 1848863461109399552
author El Moudaka, Tarek
Murugan, Priya
Abdul Rahman, Mohd Basyaruddin
Tejo, Bimo Ario
author_facet El Moudaka, Tarek
Murugan, Priya
Abdul Rahman, Mohd Basyaruddin
Tejo, Bimo Ario
author_sort El Moudaka, Tarek
building UPM Institutional Repository
collection Online Access
description Tuberculosis (TB) remains a serious threat to human health with the advent of multi-drug resistant tuberculosis (MDR-TB) and extensively drug-resistant tuberculosis (XDR-TB). The urge to find novel drugs to deal with the appearance of drug-resistant TB and its variants is highly needed. This study aims to find new CYP121 inhibitors by screening 8,773 compounds from the drug repositioning database RepoDB. The selection of CYP121 potential inhibitors was based on two criteria: the new inhibitor should bind to CYP121 with higher affinity than its original ligand and interact with catalytically important residues for the function of CYP121. The ligands were docked onto CYP121 using AutoDock Vina, and the molecular dynamics simulation of the selected ligand was conducted using YASARA Structure. We found that antrafenine, an anti-inflammatory and analgesic agent with high CYP inhibitory promiscuity, was bound to CYP121 with a binding affinity of -12.6 kcal/mol and interacted with important residues at the CYP121 binding site. Molecular dynamics analysis of CYP121 bound to the original ligand and antrafenine showed that both ligands affected the dynamics of residues located distantly from the active site. Antrafenine caused more structural changes to CYP121 than the original ligand, as indicated by a significantly higher number of affected residues and rigid body movements caused by the binding of antrafenine to CYP121.
first_indexed 2025-11-15T13:33:17Z
format Article
id upm-100974
institution Universiti Putra Malaysia
institution_category Local University
language English
last_indexed 2025-11-15T13:33:17Z
publishDate 2022
publisher Universiti Putra Malaysia Press
recordtype eprints
repository_type Digital Repository
spelling upm-1009742023-07-13T07:44:56Z http://psasir.upm.edu.my/id/eprint/100974/ Discovery of Mycobacterium tuberculosis CYP121 new inhibitor via structure-based drug repurposing El Moudaka, Tarek Murugan, Priya Abdul Rahman, Mohd Basyaruddin Tejo, Bimo Ario Tuberculosis (TB) remains a serious threat to human health with the advent of multi-drug resistant tuberculosis (MDR-TB) and extensively drug-resistant tuberculosis (XDR-TB). The urge to find novel drugs to deal with the appearance of drug-resistant TB and its variants is highly needed. This study aims to find new CYP121 inhibitors by screening 8,773 compounds from the drug repositioning database RepoDB. The selection of CYP121 potential inhibitors was based on two criteria: the new inhibitor should bind to CYP121 with higher affinity than its original ligand and interact with catalytically important residues for the function of CYP121. The ligands were docked onto CYP121 using AutoDock Vina, and the molecular dynamics simulation of the selected ligand was conducted using YASARA Structure. We found that antrafenine, an anti-inflammatory and analgesic agent with high CYP inhibitory promiscuity, was bound to CYP121 with a binding affinity of -12.6 kcal/mol and interacted with important residues at the CYP121 binding site. Molecular dynamics analysis of CYP121 bound to the original ligand and antrafenine showed that both ligands affected the dynamics of residues located distantly from the active site. Antrafenine caused more structural changes to CYP121 than the original ligand, as indicated by a significantly higher number of affected residues and rigid body movements caused by the binding of antrafenine to CYP121. Universiti Putra Malaysia Press 2022-03-31 Article PeerReviewed text en http://psasir.upm.edu.my/id/eprint/100974/1/Discovery%20of%20Mycobacterium%20tuberculosis%20.pdf El Moudaka, Tarek and Murugan, Priya and Abdul Rahman, Mohd Basyaruddin and Tejo, Bimo Ario (2022) Discovery of Mycobacterium tuberculosis CYP121 new inhibitor via structure-based drug repurposing. Pertanika Journal of Science & Technology, 31 (3). art. no. 21. pp. 1503-1521. ISSN 0128-7680; ESSN: 2231-8526 http://www.pertanika.upm.edu.my/pjst/browse/regular-issue?article=JST-3830-2022 10.47836/pjst.31.3.21
spellingShingle El Moudaka, Tarek
Murugan, Priya
Abdul Rahman, Mohd Basyaruddin
Tejo, Bimo Ario
Discovery of Mycobacterium tuberculosis CYP121 new inhibitor via structure-based drug repurposing
title Discovery of Mycobacterium tuberculosis CYP121 new inhibitor via structure-based drug repurposing
title_full Discovery of Mycobacterium tuberculosis CYP121 new inhibitor via structure-based drug repurposing
title_fullStr Discovery of Mycobacterium tuberculosis CYP121 new inhibitor via structure-based drug repurposing
title_full_unstemmed Discovery of Mycobacterium tuberculosis CYP121 new inhibitor via structure-based drug repurposing
title_short Discovery of Mycobacterium tuberculosis CYP121 new inhibitor via structure-based drug repurposing
title_sort discovery of mycobacterium tuberculosis cyp121 new inhibitor via structure-based drug repurposing
url http://psasir.upm.edu.my/id/eprint/100974/
http://psasir.upm.edu.my/id/eprint/100974/
http://psasir.upm.edu.my/id/eprint/100974/
http://psasir.upm.edu.my/id/eprint/100974/1/Discovery%20of%20Mycobacterium%20tuberculosis%20.pdf