Evidence map›Paper›PMID 40612000›Full record

ArticleBiochemistry and biophysics reports2025

Targeting tryparedoxin-dependent peroxidase (TXNPx) enzyme to identify repurposing drug candidates from FDA-approved drugs and natural products using virtual screening, ADME/Tox and MD simulations.

Eman Shorog, Sabina Yasmin, Rani Mansuri, Arpit Raj, Mohammad Ovais Dar, Sumel Ashique, Qazi Mohammad Sajid Jamal, Ali H Alharbi, Mushtaq Ahmad Wani, Mohammad Yousuf Ansari

Abstract read
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Article in Biochemistry and biophysics reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

10 authors.

Eman ShorogDepartment of Clinical Pharmacy, College of Pharmacy, King Khalid University, Abha, 62529, Saudi Arabia.
Sabina YasminDepartment of Pharmaceutical Chemistry, College of Pharmacy, King Khalid University, Abha, 62529, Saudi Arabia.
Rani MansuriSchool of Pharmaceutical Sciences, Apeejay Stya University, Gurgaon, Haryana, 122103, India.
Arpit RajSchool of Pharmaceutical Sciences, Apeejay Stya University, Gurgaon, Haryana, 122103, India.
Mohammad Ovais DarMM College of Pharmacy, Maharishi Markandeshwar (Deemed to be University), Mullana, Ambala, Haryana, India.
Sumel AshiqueDepartment of Pharmaceutical Technology, Bharat Technology, Uluberia, 711316, West Bengal, India.
Qazi Mohammad Sajid JamalDepartment of Health Informatics, College of Applied Medical Sciences, Qassim University, Buraydah, Saudi Arabia.
Ali H AlharbiDepartment of Health Informatics, College of Applied Medical Sciences, Qassim University, Buraydah, Saudi Arabia.
Mushtaq Ahmad WaniDepartment of Pharmacoinformatics, National Institute of Pharmaceutical Education and Research (NIPER), Sector 67, S.A.S. Nagar, 160062, Punjab, India.
Mohammad Yousuf AnsariMM College of Pharmacy, Maharishi Markandeshwar (Deemed to be University), Mullana, Ambala, Haryana, India.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protozoan are parasitic organisms that can cause significant diseases worldwide, such as Chagas disease, African sleeping sickness, and Leishmaniasis. In this study, we performed docking studies on type II tryparedoxin-dependent peroxidase (PDB ID: 2VUP) using a Zinc database having natural products library and FDA-approved drugs. The top compounds identified are F1762-0560, F1855-0030, FDA_339, FDA_461, tetrahydrobenzo-tetraphenoxirene, and ketoconazole. These compounds were further performed the molecular dynamics simulations studies. The docking results has suggested that top Docking Scores compounds are F17620560 (-8.6 kcal/mol), F1855-0030(-7.8 kcal/mol), FDA_339 (-7.0 kcal/mol), FDA_461 (-7.0 kcal/mol), tetrahydrobenzo-tetraphenoxirene (-7.5 kcal/mol) and, ketoconazole (-6.7 kcal/mol). The common binding affinity amino acids are SER 37, LYS 38, CYS 39, LYS 43, GLU 81 and PHE 85. The top scoring compounds (F1762-0560) has showed interactions with the target protein through hydrogen bonding and stacking interactions, particularly with SER 37, CYS 39, and LYS 43. We further investigated the stability of six ligand-TXNPx complexes over 200 ns. The results indicated good structural stability (RMSD: 0.05-0.20 nm; Rg: 1.45-1.52 nm), with F0556-0242 and F1762-0560 showing the least fluctuations. FDA_461 has the most hydrogen bonds (up to 5), while Ketoconazole was more flexible (RMSD peak: 0.25 nm). These findings suggest that F0556-0242, F1762-0560, and FDA_461 are promising candidates.

Indexed as

Binding affinityDocking studiesMolecular dynamicsProtozoaType II tryparedoxin-dependent peroxidase

Identifiers

PMID40612000
PMCPMC12221838

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