Structure-antiviral activity relationships of cecropin A-magainin 2 hybrid peptide and its analogues. |
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Authors: | Dong Gun Lee Yoonkyung Park Ingnyol Jin Kyung-Soo Hahm Hyang-Hee Lee Young-Hee Moon Eun-Rhan Woo |
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Affiliation: | School of Life Science and Biotechnology, College of Natural Sciences, Kyungpook National University, 1370 Sankyuk-dong, Puk-ku, Taegu 702-701, Korea. |
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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. |
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Keywords: | antiviral activity cecropin A (1–8)‐magainin 2 (1–12) hydrophobicity |
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