Effects of Amino Acid Deletion and Substitution on the Chemical Properties, Biological Activities of the Frog Peptide Palustrin-OG1
2013
Palustrin-OG1 (OG1) is a host defense peptide isolated from the frog Odorrana grahami. In this study, we analyzed
the chemical properties, antimicrobial activities and cytotoxicities of OG1 and its derivatives to identify the most
promising peptide as an antimicrobial agent. By increasing the net positive charge, amphipathicity and decreasing the
mean hydrophobicity of OG1, the derivative named as OG2 exerted higher antimicrobial activity against bacteria but
lower cytotoxicity against both porcine erythrocytes and peripheral blood mononuclear cells than did OG1 (P<0.01). After
substitution of Cys residues of OG2 by Ala or Trp residues, two derivatives named as OG2A and OG2W were less effective
against bacteria and induced greater hemolysis than did OG2, indicating the importance of Cys residues. The substitution
of the C-terminal Thr of OG2 resulted OG2N, which decreased the cytotoxicity and improved killing kinetics against
gram-positive bacteria by the rapid damage of cell wall and membrane.
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