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From proteome to potential drugs: integration of subtractive proteomics and ensemble docking for drug repurposing against Pseudomonas aeruginosa RND superfamily proteins

dc.contributor.authorUrra, Gabriela
dc.contributor.authorValdés-Muñoz, Elizabeth
dc.contributor.authorSuardiaz, Reynier
dc.contributor.authorHernández-Rodríguez, Erix W.
dc.contributor.authorPalma, Jonathan M.
dc.contributor.authorRíos-Rozas, Sofía E.
dc.contributor.authorFlores-Morales, Camila A.
dc.contributor.authorAlegría-Arcos, Melissa
dc.contributor.authorYáñez, Osvaldo
dc.contributor.authorMorales-Quintana, Luis
dc.contributor.authorD’Afonseca, Vívian
dc.contributor.authorBustos, Daniel
dc.date.accessioned2024-09-10T13:31:12Z
dc.date.available2024-09-10T13:31:12Z
dc.date.issued2024
dc.identifier.urihttp://repositorio.ucm.cl/handle/ucm/5651
dc.description.abstractPseudomonas aeruginosa (P. aeruginosa) poses a significant threat as a nosocomial pathogen due to its robust resistance mechanisms and virulence factors. This study integrates subtractive proteomics and ensemble docking to identify and characterize essential proteins in P. aeruginosa, aiming to discover therapeutic targets and repurpose commercial existing drugs. Using subtractive proteomics, we refined the dataset to discard redundant proteins and minimize potential cross-interactions with human proteins and the microbiome proteins. We identified 12 key proteins, including a histidine kinase and members of the RND efflux pump family, known for their roles in antibiotic resistance, virulence, and antigenicity. Predictive modeling of the three-dimensional structures of these RND proteins and subsequent molecular ensemble-docking simulations led to the identification of MK-3207, R-428, and Suramin as promising inhibitor candidates. These compounds demonstrated high binding affinities and effective inhibition across multiple metrics. Further refinement using non-covalent interaction index methods provided deeper insights into the electronic effects in protein–ligand interactions, with Suramin exhibiting superior binding energies, suggesting its broad-spectrum inhibitory potential. Our findings confirm the critical role of RND efflux pumps in antibiotic resistance and suggest that MK-3207, R-428, and Suramin could be effectively repurposed to target these proteins. This approach highlights the potential of drug repurposing as a viable strategy to combat P. aeruginosa infections.es_CL
dc.language.isoenes_CL
dc.rightsAtribución-NoComercial-SinDerivadas 3.0 Chile*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/cl/*
dc.sourceInternational Journal of Molecular Sciences, 25(15), 8027es_CL
dc.subjectAntimicrobial resistancees_CL
dc.subjectEfflux pumpes_CL
dc.subjectEnsemble-dockinges_CL
dc.subjectDrug repurposinges_CL
dc.subjectPseudomonas aeruginosa;es_CL
dc.subjectSubtractive proteomicses_CL
dc.subjectRND superfamilyes_CL
dc.titleFrom proteome to potential drugs: integration of subtractive proteomics and ensemble docking for drug repurposing against Pseudomonas aeruginosa RND superfamily proteinses_CL
dc.typeArticlees_CL
dc.ucm.facultadFacultad de Ciencias Agrarias y Forestaleses_CL
dc.ucm.indexacionScopuses_CL
dc.ucm.indexacionIsies_CL
dc.ucm.urimdpi.com/1422-0067/25/15/8027es_CL
dc.ucm.doidoi.org/10.3390/ijms25158027es_CL


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Atribución-NoComercial-SinDerivadas 3.0 Chile
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