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Structure–antiviral activity relationships of cecropin A‐magainin 2 hybrid peptide and its analogues
Author(s) -
Lee Dong Gun,
Park Yoonkyung,
Jin Ingnyol,
Hahm KyungSoo,
Lee HyangHee,
Moon YoungHee,
Woo EunRhan
Publication year - 2004
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.504
Subject(s) - magainin , peptide , amino acid , chemistry , residue (chemistry) , stereochemistry , cecropin , biochemistry , structure–activity relationship , peptide sequence , serine , antimicrobial peptides , in vitro , gene , enzyme
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.