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

作者：Souza Andre L A; Diaz Dellavalle Paola; Cabrera Andrea; Larranaga Patricia; Dalla Rizza Marco; De Simone Salvatore G^*

来源：Peptides, 2013, 45: 78-84.

DOI：10.1016/j.peptides.2013.03.030

• Pleurocidin
• Antimicrobial peptides
• Antifungal activity
• Cationic peptides
• Pore-forming
• Synthetic peptides
• Small active sequence

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.

• 出版日期2013-7