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Ib-M6 antimicrobial peptide: Antibacterial activity against clinical isolates of Escherichia coli and molecular docking

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dc.contributor.authorFlórez Castillo, Johanna-Marcela
dc.contributor.authorRondón Villarreal, Paola
dc.contributor.authorRopero Vega, José Luis
dc.contributor.authorMendoza Espinel, Stephany Y.
dc.contributor.authorMoreno Amézquita, July A.
dc.contributor.authorMéndez Jaimes, Karen D.
dc.contributor.authorFarfán García, Ana Elvira
dc.contributor.authorGómez Rangel, Sergio-Yebrail
dc.contributor.authorGómez Duarte, Oscar Gilberto
dc.contributor.researchgroupCLINIUDESspa
dc.contributor.researchgroupCIBASspa
dc.date.accessioned2021-10-06T15:11:38Z
dc.date.available2021-10-06T15:11:38Z
dc.date.issued2020-03-12
dc.descriptionDigitalspa
dc.description.abstractThe Ib-M6 peptide has antibacterial activity against non-pathogenic Escherichia coli K-12 strain. The first part of this study determines the antibacterial activity of Ib-M6 against fourteen pathogenic strains of E. coli O157:H7. Susceptibility assay showed that Ib-M6 had values of Minimum Inhibitory Concentration (MIC) lower than streptomycin, used as a reference antibiotic. Moreover, to predict the possible interaction between Ib-M6 and outer membrane components of E. coli, we used molecular docking simulations where FhuA protein and its complex with Lipopolysaccharide (LPS–FhuA) were used as targets of the peptide. FhuA/Ib-M6 complexes had energy values between −39.5 and −40.5 Rosetta Energy Units (REU) and only one hydrogen bond. In contrast, complexes between LPS–FhuA and Ib-M6 displayed energy values between −25.6 and −40.6 REU, and the presence of five possible hydrogen bonds. Hence, the antimicrobial activity of Ib-M6 peptide shown in the experimental assays could be caused by its interaction with the outer membrane of E. coli. View Full-Textspa
dc.description.researchareaCiencias básicas biomédicas, epidemiología, salud pública enfermedades infecciosas, enfermedades no transmisibles epidemiología, salud y desarrollo, discapacidadspa
dc.description.researchareaCiencias Básicas y Aplicadas para la Sostenibilidadspa
dc.format.extent1 p.spa
dc.format.mimetypeapplication/pdfspa
dc.identifier.doi10.3390/antibiotics9020079
dc.identifier.urihttps://repositorio.udes.edu.co/handle/001/5665
dc.language.isoengspa
dc.publisher.placeSuizaspa
dc.relation.citationissue2, febrero de 2020spa
dc.relation.citationvolume9spa
dc.relation.citesFlórez-Castillo, J.M.; Rondón-Villareal, P.; Ropero-Vega, J.L.; Mendoza-Espinel, S.Y.; Moreno-Amézquita, J.A.; Méndez-Jaimes, K.D.; Farfán-García, A.E.; Gómez-Rangel, S.Y.; Gómez-Duarte, O.G. Ib-M6 Antimicrobial Peptide: Antibacterial Activity against Clinical Isolates of Escherichia coli and Molecular Docking. Antibiotics 2020, 9, 79. https://doi.org/10.3390/antibiotics9020079
dc.relation.indexedAntibiotics 2020, 9, 79; doi:10.3390/antibiotics9020079spa
dc.relation.ispartofjournalAntibioticsspa
dc.rightsThe Editor(s) and the Author(s), 2020spa
dc.rights.accessrightsinfo:eu-repo/semantics/openAccessspa
dc.rights.creativecommonsAtribución-NoComercial 4.0 Internacional (CC BY-NC 4.0)spa
dc.rights.urihttps://creativecommons.org/licenses/by-nc/4.0/spa
dc.sourcehttps://www.mdpi.com/2079-6382/9/2/79#framed_div_cited_countspa
dc.subject.proposalAntimicrobial peptideseng
dc.subject.proposalEscherichia colieng
dc.subject.proposalMolecular dockingeng
dc.titleIb-M6 antimicrobial peptide: Antibacterial activity against clinical isolates of Escherichia coli and molecular dockingspa
dc.typeArtículo de revistaspa
dc.type.coarhttp://purl.org/coar/resource_type/c_6501spa
dc.type.contentTextspa
dc.type.driverinfo:eu-repo/semantics/articlespa
dc.type.redcolhttp://purl.org/redcol/resource_type/ARTspa
dc.type.versioninfo:eu-repo/semantics/publishedVersionspa
dcterms.audienceTodas las Audienciasspa
dspace.entity.typePublication
oaire.accessrightshttp://purl.org/coar/access_right/c_abf2spa
oaire.versionhttp://purl.org/coar/version/c_970fb48d4fbd8a85spa
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