1. Academic Validation
  2. Structure-function relationships in bombinins H, antimicrobial peptides from Bombina skin secretions

Structure-function relationships in bombinins H, antimicrobial peptides from Bombina skin secretions

  • Peptides. 2000 Nov;21(11):1673-9. doi: 10.1016/s0196-9781(00)00316-8.
M L Mangoni 1 N Grovale A Giorgi G Mignogna M Simmaco D Barra
Affiliations

Affiliation

  • 1 Dipartimento di Scienze Biomediche, Università 'G. d'Annunzio', 66100, Chieti, Italy.
Abstract

Skin secretions of amphibia of the Bombina genus contain two families of antimicrobial Peptides, the bombinins (bombinin-like Peptides) and the bombinins H (H for hydrophobic and hemolytic). The latter family includes a number of Peptides containing a D-amino acid in the second position, in addition to their corresponding all L-isomers. The antimicrobial activity of three pairs of bombinin H isomers, H2/H4, H6/H7 and GH-1D/GH-1L, has been investigated. The first two pairs of Peptides were actually isolated from the secretion, whereas the third was synthesized according to the sequence deduced from a gene coding for a bombinin-like peptide in Bombina orientalis.

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