Structure–antiviral activity relationships of cecropin A-magainin 2 hybrid peptide and its analogues

✍ Scribed by Dong Gun Lee; Yoonkyung Park; Ingnyol Jin; Kyung-Soo Hahm; Hyang-Hee Lee; Young-Hee Moon; Dr Eun-Rhan Woo

• Publisher: John Wiley and Sons
• Year: 2004
• Tongue: English
• Weight: 186 KB
• Volume: 10
• Category: Article
• ISSN: 1075-2617
• DOI: 10.1002/psc.504

✦ Synopsis

Abstract

In order to elucidate the structure–antiviral activity relationship of cecropin A (1–8)‐magainin 2 (1–12) (termed CA‐MA) hybrid peptide, several analogues with amino acid substitutions were synthesized. In a previous study, it was shown that serine at position 16 in CA‐MA hybrid peptide was very important for antimicrobial activity. Analogues were designed to increase the hydrophobic property by substituting a hydrophobic amino acid residue (S→A, V, F or W, position 16) in the CA‐MA hybrid peptide. In this study, the structure–antiviral activity relationships of CA‐MA and its analogues were investigated. In particular, substitution of Ser with a hydrophobic amino acid, Val, Phe or Trp at position 16 caused a dramatic increase in the virus–cell fusion inhibitory activity. These results suggested that the hydrophobicity at position 16 in the hydrophobic region of CA‐MA is important for potent antiviral activity. Copyright © 2003 European Peptide Society and John Wiley & Sons, Ltd.