Article
Antimicrobial activity of pleurocidin is retained in Plc-2, a C-terminal 12-amino acid fragment
Registro en:
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.
0196-9781
10.1016/j.peptides.2013.03.030
Autor
Souza, Andre L. A.
Dellavalle, Paola Diaz
Cabrera, Andrea
Larrañaga, Patricia
Rizza, Marco Dalla
De Simone, Salvatore Giovanni
Resumen
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.