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NMR structure of mussel mytilin, and antiviral-antibacterial activities of derived synthetic peptides ArchiMer
Roch, Philippe; Yang, Y; Toubiana, Mylene; Aumelas, A.
Mytilin is a 34-residue antibacterial peptide from the mussel Mytilus galloprovincialis, which in addition possesses in vitro antiviral activity. The three-dimensional solution structure of the synthetic mytilin was established by using 1H NMR and consists of the common cysteine-stabilized alpha beta motif close to the one observed in the mussel defensin MGD-1. Mytilin is characterized by 8 cysteines engaged in four disulfide bonds (2-27, 6-29, 10-31, and 15-34) only involving the beta-strand II. Hydrophilic and hydrophobic areas of mytilin account for 63% and 37%, respectively, a ratio very close to that of MGD-1 (64% and 36%). One linear and three cyclic fragments were designed from the interstrand loop sequence known to retain the biological activities...
Tipo: Text Palavras-chave: Shrimp; Molluscs; Mussel; Antibacterial activity; WSSV; Viral protection; Beta hairpin structure; NMR; Mytilin; Antimicrobial peptide.
Ano: 2008 URL:
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