| Author | Souza, Andre L. A. | |
| Author | Dellavalle, Paola Diaz | |
| Author | Cabrera, Andrea | |
| Author | Larrañaga, Patricia | |
| Author | Rizza, Marco Dalla | |
| Author | De Simone, Salvatore Giovanni | |
| Access date | 2015-08-19T13:49:29Z | |
| Available date | 2015-08-19T13:49:29Z | |
| Document date | 2013 | |
| Citation | SOUZA, 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. | pt_BR |
| ISSN | 0196-9781 | pt_BR |
| URI | https://www.arca.fiocruz.br/handle/icict/11537 | |
| Language | eng | pt_BR |
| Publisher | Elsevier | pt_BR |
| Rights | restricted access | |
| Title | Antimicrobial activity of pleurocidin is retained in Plc-2, a C-terminal 12-amino acid fragment | pt_BR |
| Type | Article | |
| DOI | 10.1016/j.peptides.2013.03.030 | pt_BR |
| Abstract | An 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. | pt_BR |
| Affilliation | Fundação Oswaldo Cruz. Centro de Desenvolvimento Tecnológico em Saúde (CDTS). Instituto Nacional de Ciência e Tecnologia para Inovação em Doenças Negligenciadas. Rio de Janeiro, RJ, Brasil | pt_BR |
| Affilliation | Biotechnology Unit. Laboratory of Proteins. INIA Las Brujas. Canelones, Uruguay. | pt_BR |
| Affilliation | Biotechnology Unit. Laboratory of Proteins. INIA Las Brujas. Canelones, Uruguay. | pt_BR |
| Affilliation | Biotechnology Unit. Laboratory of Proteins. INIA Las Brujas. Canelones, Uruguay. | pt_BR |
| Affilliation | Biotechnology Unit. Laboratory of Proteins. INIA Las Brujas. Canelones, Uruguay. | pt_BR |
| Affilliation | Fundação Oswaldo Cruz. Centro de Desenvolvimento Tecnológico em Saúde (CDTS). Instituto Nacional de Ciência e Tecnologia para Inovação em Doenças Negligenciadas. Rio de Janeiro, RJ, Brasil /Universidade Federal Fluminense. Departamento de Biologia Celular e Molecular. Niterói, RJ, Brasil / Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Bioquímica de Proteinas e Peptídeos. Rio de Janeiro, RJ, Brasil. | pt_BR |
| Subject | Pleurocidin | pt_BR |
| Subject | Antimicrobial peptides | pt_BR |
| Subject | Antifungal activity | pt_BR |
| Subject | Cationic peptides | pt_BR |
| Subject | Pore-forming | pt_BR |
| Subject | Synthetic peptides | pt_BR |
| Subject | Small active sequence | pt_BR |
| DeCS | Peptídeos | pt_BR |
| DeCS | Anticorpos Antifúngicos | pt_BR |
| DeCS | Peptídeos Catiônicos Antimicrobianos | pt_BR |
