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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Anti-Infective Agents / chemical synthesis
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Anti-Infective Agents / pharmacology*
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Antimicrobial Cationic Peptides / chemical synthesis
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Antimicrobial Cationic Peptides / pharmacology*
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CD4 Antigens / genetics
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CD4 Antigens / metabolism
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Chlorocebus aethiops
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Giant Cells / drug effects
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HIV Envelope Protein gp120 / genetics
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HIV Envelope Protein gp120 / metabolism*
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HIV Envelope Protein gp41 / genetics
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HIV Envelope Protein gp41 / metabolism*
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HIV-1 / genetics
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HIV-1 / metabolism*
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HeLa Cells
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Humans
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Magainins
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Recombinant Fusion Proteins / chemical synthesis
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Recombinant Fusion Proteins / pharmacology*
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Structure-Activity Relationship*
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Vaccinia virus / genetics
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Vero Cells
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Xenopus Proteins / chemical synthesis
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Xenopus Proteins / pharmacology*
Substances
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Anti-Infective Agents
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Antimicrobial Cationic Peptides
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CD4 Antigens
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HIV Envelope Protein gp120
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HIV Envelope Protein gp41
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Magainins
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Recombinant Fusion Proteins
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Xenopus Proteins
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magainin 2 peptide, Xenopus
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cecropin A