<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Farfan-Garcia AE</submitter><funding>Ministerio de Ciencia, TecnologÃa e InnovaciÃ³n</funding><pagination>e0334029</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC12507217</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>20(10)</volume><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</pubmed_abstract><journal>PloS one</journal><pubmed_title>Structural and functional analysis of Escherichia coli membrane disruption by Ib-M peptides.</pubmed_title><pmcid>PMC12507217</pmcid><funding_grant_id>129980763392 CT-760-2018</funding_grant_id><pubmed_authors>Farfan-Garcia AE</pubmed_authors><pubmed_authors>Gomez-Duarte OG</pubmed_authors><pubmed_authors>Rincon-Baron EJ</pubmed_authors><pubmed_authors>Hernandez-Penaranda IP</pubmed_authors><pubmed_authors>Florez-Castillo JM</pubmed_authors><pubmed_authors>Torres-Rodriguez GA</pubmed_authors></additional><is_claimable>false</is_claimable><name>Structural and functional analysis of Escherichia coli membrane disruption by Ib-M peptides.</name><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</description><dates><release>2025-01-01T00:00:00Z</release><publication>2025</publication><modification>2026-06-04T08:47:28.492Z</modification><creation>2026-05-07T03:12:16.956Z</creation></dates><accession>S-EPMC12507217</accession><cross_references><pubmed>41061016</pubmed><doi>10.1371/journal.pone.0334029</doi></cross_references></HashMap>