Influence of N-terminus modifications on the biological activity, membrane interaction, and secondary structure of the antimicrobial peptide hylin-a1

• Published in: Biopolymers Vol. 96; no. 1; pp. 41 - 48
• Main Authors: Crusca Jr, Edson, Rezende, Adrielle A., Marchetto, Reinaldo, Mendes-Giannini, Maria J. S., Fontes, Wagner, Castro, Mariana S., Cilli, Eduardo M.
• Format: Journal Article
• Language: English
• Published: Hoboken Wiley Subscription Services, Inc., A Wiley Company 2011
• Subjects: Amino Acid Sequence; Amphibian Proteins - chemistry; Amphibian Proteins - metabolism; Amphibian Proteins - pharmacology; Animals; Anti-Infective Agents - chemistry; Anti-Infective Agents - metabolism; Anti-Infective Agents - pharmacology; antimicrobial peptide; Anura - metabolism; Bacteria - drug effects; Bacteria - growth & development; Circular Dichroism; Fungi - drug effects; Fungi - growth & development; Hemolysis - drug effects; Humans; Hydrophobic and Hydrophilic Interactions; hypsiboas; Lipid Bilayers - chemistry; Lipid Bilayers - metabolism; Microbial Sensitivity Tests; Molecular Sequence Data; Peptides - chemistry; Peptides - metabolism; Peptides - pharmacology; Protein Structure, Secondary; SPPS-Fmoc

Recently the peptide Hy‐a1 (IFGAILPLALGALKNLIK), with antimicrobial activity, was isolated from the skin secretion of the frog Hypsiboas albopunctatus. The aim of the present work was to evaluate four analogues with introduction of acetyl group, Asp or Lys at the N‐terminus of antimicrobial peptide...