| 1. |
Gervacio-Villarreal E.♦, Ropón-Palacios G.♦, Sancho C.♦, Pérez-Silva J.♦, Otazu K.♦, Olivos Ramirez G., Vega-Chozo K.♦, Ramirez-Díaz Y.L.♦, Chenet-Zuta M.E.♦, Navarro del Aguila I.♦, De la Cruz Flores M.♦, Aguiar C.♦, Camps I.♦, Ensemble Docking of FDA-Approved and Peruvian Phytochemicals Against Monkeypox Virus Telomere-Binding Protein,
ChemistrySelect, ISSN: 2365-6549, DOI: 10.1002/slct.202504269, Vol.11, No.9, pp.e04269-1-21, 2026 Abstract:
Monkeypox is a reemerging zoonotic disease that has been spreading worldwide. Different approaches are being conducted to find effective treatments for this disease. To accelerate therapeutic discovery, we propose telomere-binding protein (TBP) as a potential drug target because of its important role during virus maturation. Using computational biology and biophysics techniques, the MPXV TBP was modeled, and a library of FDA-approved drugs and phytocompounds was screened using a rigorous ensemble docking protocol; conformational sampling was enhanced by enumerating, for each ligand, ionization states, tautomerism, and ring conformations. Our results present a new approach to drug selection against MPXV, with six potential inhibitors: CHEMBL3894860, CHEMBL461101, CHEMBL2103870, PNSC125, PNSC305, and PNSC123, which can be taken as lead compounds for experimental testing, for example, in plaque reduction assays and qPCR in MPXV-infected cells to determine EC50, CC50, and selectivity index (SI) values. Keywords:
drug screening, ensemble docking, Monkeypox virus, telomere binding protein Affiliations:
| Gervacio-Villarreal E. | - | other affiliation | | Ropón-Palacios G. | - | other affiliation | | Sancho C. | - | other affiliation | | Pérez-Silva J. | - | other affiliation | | Otazu K. | - | other affiliation | | Olivos Ramirez G. | - | IPPT PAN | | Vega-Chozo K. | - | other affiliation | | Ramirez-Díaz Y.L. | - | other affiliation | | Chenet-Zuta M.E. | - | other affiliation | | Navarro del Aguila I. | - | other affiliation | | De la Cruz Flores M. | - | other affiliation | | Aguiar C. | - | other affiliation | | Camps I. | - | other affiliation |
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| 2. |
Otazu K.♦, Olivos Ramirez G.♦, Fernández-Silva P.♦, Vilca-Quispe J.♦, Vega-Chozo K.♦, Jimenez-Avalos G.♦, Chenet-Zuta M. E.♦, Sosa-Amay F. E.♦, Cárdenas Cárdenas R. G.♦, Ropón-Palacios G.♦, Dattani N.♦, Camps I.♦, The Malaria Box molecules: a source for targeting the RBD and NTD cryptic pocket of the spike glycoprotein in SARS-CoV-2,
Journal of Molecular Modeling, ISSN: 1610-2940, DOI: 10.1007/s00894-024-06006-y, Vol.30, pp.217-1-21, 2024Abstract:
Context
SARS-CoV-2, responsible for COVID-19, has led to over 500 million infections and more than 6 million deaths globally. There have been limited effective treatments available. The study aims to find a drug that can prevent the virus from entering host cells by targeting specific sites on the virus’s spike protein.
Method
We examined 13,397 compounds from the Malaria Box library against two specific sites on the spike protein: the receptor-binding domain (RBD) and a predicted cryptic pocket. Using virtual screening, molecular docking, molecular dynamics, and MMPBSA techniques, they evaluated the stability of two compounds. TCMDC-124223 showed high stability and binding energy in the RBD, while TCMDC-133766 had better binding energy in the cryptic pocket. The study also identified that the interacting residues are conserved, which is crucial for addressing various virus variants. The findings provide insights into the potential of small molecules as drugs against the spike protein. Keywords:
SARS-CoV-2, Molecular docking, Spike protein, Cryptic pocket, MMPBSA Affiliations:
| Otazu K. | - | other affiliation | | Olivos Ramirez G. | - | other affiliation | | Fernández-Silva P. | - | other affiliation | | Vilca-Quispe J. | - | other affiliation | | Vega-Chozo K. | - | other affiliation | | Jimenez-Avalos G. | - | other affiliation | | Chenet-Zuta M. E. | - | other affiliation | | Sosa-Amay F. E. | - | other affiliation | | Cárdenas Cárdenas R. G. | - | other affiliation | | Ropón-Palacios G. | - | other affiliation | | Dattani N. | - | other affiliation | | Camps I. | - | other affiliation |
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