Antimicrobial activity of pleurocidin is retained in Plc-2, a C-terminal 12-amino acid fragment |
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Institution: | 1. National Institute of Science and Technology on Innovation on Neglected Diseases (INCT-IDN)/Center for Technological Development in Health (CDTS), FIOCRUZ, Rio de Janeiro, RJ, Brazil;2. Department of Molecular and Cell Biology, Federal Fluminense University, Niterói, RJ, Brazil;3. Laboratory of Proteins, Biotechnology Unit, INIA Las Brujas, Canelones, Uruguay;4. Protein and Peptides Laboratory Oswaldo Cruz Institute, FIOCRUZ, Rio de Janeiro, RJ, Brazil |
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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. |
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Keywords: | Pleurocidin Antimicrobial peptides Antifungal activity Cationic peptides Pore-forming Synthetic peptides Small active sequence |
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