Ítem
Acceso Abierto

A new synthetic peptide having two target of antibacterial action in E. coli ML35

Mostrar el registro sencillo de la publicación
dc.creatorBarreto-Santamaría, Adriana
dc.creatorCurtidor, Hernando
dc.creatorArévalo-Pinzón, Gabriela
dc.creatorHerrera, Chonny
dc.creatorSuárez, Diana
dc.creatorPérez, Walter H.
dc.creatorPatarroyo, Manuel E.
dc.creator.googleBarreto-Santamaría, Adrianaspa
dc.creator.googleCurtidor, Hernandospa
dc.creator.googleArévalo-Pinzón, Gabrielaspa
dc.creator.googleHerrera, Chonnyspa
dc.creator.googleSuárez, Dianaspa
dc.creator.googlePérez, Walter H.spa
dc.creator.googlePatarroyo, Manuel E.spa
dc.date.accessioned2019-02-26T16:11:19Z
dc.date.available2019-02-26T16:11:19Z
dc.date.created2016
dc.date.issued2016
dc.description.abstractThe increased resistance of microorganisms to the different antimicrobials available to today has highlighted the need to find new therapeutic agents, including natural and/or synthetic antimicrobial peptides (AMPs). This study has evaluated the antimicrobial activity of synthetic peptide 35409 (RYRRKKKMKKALQYIKLLKE) against Staphylococcus aureus ATCC 29213, Pseudomonas aeruginosa ATCC 15442 and Escherichia coli ML 35 (ATCC 43827). The results have shown that peptide 35409 inhibited the growth of these three bacterial strains, having 16-fold greater activity against E. coli and P. aeruginosa, but requiring less concentration regarding E. coli (22 μM). When analyzing this activity against E. coli compared to time taken, it was found that this peptide inhibited bacterial growth during the first 60 min and reduced CFU/mL 1 log after 120 min had elapsed. This AMP permeabilized the E. coli membrane by interaction with membrane phospholipids, mainly phosphatidylethanolamine, inhibited cell division and induced filamentation, suggesting two different targets of action within a bacterial cell. Cytotoxicity studies revealed that peptide 35409 had low hemolytic activity and was not cytotoxic for two human cell lines. We would thus propose, in the light of these findings, that the peptide 35409 sequence should provide a promising template for designing broad-spectrum AMPs. © 2016 Barreto-Santamaría, Curtidor, Arévalo-Pinzón, Herrera, Suárez, Pérez and Patarroyo.eng
dc.format.mimetypeapplication/pdf
dc.identifier.doi10.3389/fmicb.2016.02006
dc.identifier.issn1664-302X
dc.identifier.urihttp://repository.urosario.edu.co/handle/10336/19144
dc.language.isoengspa
dc.relation.citationIssueNo. DEC
dc.relation.citationTitleFrontiers in Microbiology
dc.relation.citationVolumeVol. 7
dc.relation.ispartofFrontiers in Microbiology, ISSN: 1664-302X Vol. 7, No. DEC (2016)spa
dc.relation.urihttps://www.frontiersin.org/articles/10.3389/fmicb.2016.02006/fullspa
dc.rights.accesRightsinfo:eu-repo/semantics/openAccess
dc.rights.accesoAbierto (Texto Completo)spa
dc.source.instnameinstname:Universidad del Rosario
dc.source.reponamereponame:Repositorio Institucional EdocUR
dc.subjectPeptide 35409spa
dc.subjectPhosphatidylethanolaminespa
dc.subjectPolypeptide antibiotic agentspa
dc.subjectUnclassified drugspa
dc.subjectAntibacterial activityspa
dc.subjectBacterial growthspa
dc.subjectCell divisionspa
dc.subjectCircular dichroismspa
dc.subjectColony forming unitspa
dc.subjectControlled studyspa
dc.subjectCytotoxicityspa
dc.subjectDNA bindingspa
dc.subject.ddcBiologíaspa
dc.subject.lembPeptidosspa
dc.subject.lembMicroorganismosspa
dc.titleA new synthetic peptide having two target of antibacterial action in E. coli ML35spa
dc.typearticleeng
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.type.spaArtículospa
Archivos
Bloque original
Mostrando1 - 1 de 1
Miniatura
Nombre:
A_new_synthetic_peptide_having_two_target_of_antibacterial_action_in_E._coli_ML35.pdf
Tamaño:
1.56 MB
Formato:
Adobe Portable Document Format
Descripción:
Descargar
Colecciones
Artículos