{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Farfan-Garcia AE"],"funding":["Ministerio de Ciencia, TecnologÃa e Innovación"],"pagination":["e0334029"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12507217"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["20(10)"],"pubmed_abstract":["Antimicrobial resistance represents a critical global public health challenge, leading to increased mortality and morbidity due to the ineffectiveness of current antibiotics against bacterial infections. Antimicrobial peptides (AMPs) offer a promising alternative for treating bacterial infections because of their broad-spectrum activity, biocompatibility, and rapid bactericidal action. Recent studies have demonstrated that Ib-M peptides exhibit bactericidal activity against pathogenic Escherichia coli clinical isolates. The objective of this study was to evaluate the mechanisms by which Ib-M peptides destabilize and disrupts E. coli membranes. We showed by dilutions assays that Ib-M peptides had a minimum inhibitory concentration (MIC) of 12.5 µM against E. coli. Electron microscopy studie"],"journal":["PloS one"],"pubmed_title":["Structural and functional analysis of Escherichia coli membrane disruption by Ib-M peptides."],"pmcid":["PMC12507217"],"funding_grant_id":["129980763392 CT-760-2018"],"pubmed_authors":["Farfan-Garcia AE","Gomez-Duarte OG","Rincon-Baron EJ","Hernandez-Penaranda IP","Florez-Castillo JM","Torres-Rodriguez GA"],"additional_accession":[]},"is_claimable":false,"name":"Structural and functional analysis of Escherichia coli membrane disruption by Ib-M peptides.","description":"Antimicrobial resistance represents a critical global public health challenge, leading to increased mortality and morbidity due to the ineffectiveness of current antibiotics against bacterial infections. Antimicrobial peptides (AMPs) offer a promising alternative for treating bacterial infections because of their broad-spectrum activity, biocompatibility, and rapid bactericidal action. Recent studies have demonstrated that Ib-M peptides exhibit bactericidal activity against pathogenic Escherichia coli clinical isolates. The objective of this study was to evaluate the mechanisms by which Ib-M peptides destabilize and disrupts E. coli membranes. We showed by dilutions assays that Ib-M peptides had a minimum inhibitory concentration (MIC) of 12.5 µM against E. coli. Electron microscopy studie","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025","modification":"2026-06-04T08:47:28.492Z","creation":"2026-05-07T03:12:16.956Z"},"accession":"S-EPMC12507217","cross_references":{"pubmed":["41061016"],"doi":["10.1371/journal.pone.0334029"]}}