Antimicrobial activity of pleurocidin is retained in Plc-2, a C-terminal 12-amino acid fragment

dc.creatorSouza, Andre L. A.
dc.creatorDellavalle, Paola Diaz
dc.creatorCabrera, Andrea
dc.creatorLarrañaga, Patricia
dc.creatorRizza, Marco Dalla
dc.creatorDe Simone, Salvatore Giovanni
dc.date2015-08-19T13:49:29Z
dc.date2015-08-19T13:49:29Z
dc.date2013
dc.date.accessioned2023-09-26T20:14:44Z
dc.date.available2023-09-26T20:14:44Z
dc.identifierSOUZA, Andre L. A.; et al. Antimicrobial activity of pleurocidin is retained in Plc-2, a C-terminal 12-amino acid fragment. Peptides , v.45, p.78–84, 2013.
dc.identifier0196-9781
dc.identifierhttps://www.arca.fiocruz.br/handle/icict/11537
dc.identifier10.1016/j.peptides.2013.03.030
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8852331
dc.descriptionAn analysis of a series of five peptides composed of various portions of the pleurocidin (Plc) sequence identified a l2-amino acid fragment from the C-terminus of Plc, designated Plc-2, as the smallest fragment that retained a antimicrobial activity comparable to that of the parent compound. MIC tests in vitro with low-ionic-strength medium showed that Plc-2 has potent activity against Pseudomonas aeruginosa, Escherichia coli and Staphylococcus aureus but not against Enterococcus faecalis. The antifungal activity of the synthetic peptides against phytopathogenic fungi, such as Fusarium oxysporum, Colletotrichum sp., Aspergillus niger and Alternaria sp., also identified Plc-2 as a biologically active peptide. Microscopy studies of fluorescently stained fungi treated with Plc-2 demonstrated that cytoplasmic and nuclear membranes were compromised in all strains of phytopathogenic fungi tested. Together, these results identify Plc-2 as a potential antimicrobial agent with similar properties to its parent compound, pleurocidin. In addition, it demonstrated that the KHVGKAALTHYL residues are critical for the antimicrobial activity described for pleurocidin.
dc.formatapplication/pdf
dc.languageeng
dc.publisherElsevier
dc.rightsrestricted access
dc.subjectPleurocidin
dc.subjectAntimicrobial peptides
dc.subjectAntifungal activity
dc.subjectCationic peptides
dc.subjectPore-forming
dc.subjectSynthetic peptides
dc.subjectSmall active sequence
dc.subjectPeptídeos
dc.subjectAnticorpos Antifúngicos
dc.subjectPeptídeos Catiônicos Antimicrobianos
dc.titleAntimicrobial activity of pleurocidin is retained in Plc-2, a C-terminal 12-amino acid fragment
dc.typeArticle


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