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.
Structure-function relationships in bombinins H, antimicrobial peptides from Bombina skin secretions / Mangoni, Maria Luisa; Grovale, N.; Giorgi, Alessandra; Mignogna, Giuseppina; Simmaco, Maurizio; Barra, Donatella. - In: PEPTIDES. - ISSN 0196-9781. - STAMPA. - 21:(2000), pp. 1673-1679. [10.1016/S0196-9781(00)00316-8]
Structure-function relationships in bombinins H, antimicrobial peptides from Bombina skin secretions.
MANGONI, Maria Luisa;GIORGI, ALESSANDRA;MIGNOGNA, Giuseppina;SIMMACO, Maurizio;BARRA, Donatella
2000
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.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.