The bombinin family of antimicrobial peptides is constituted by a number of molecules isolated from skin secretions of frogs belonging to the genus Bombina. These peptides can be grouped into two distinct subfamilies: the bombinin and the bombinin H. The former comprises 27-amino-acid residue peptides with antimicrobial activity against Gram-negative and Gram-positive bacteria and fungi; the latter includes 20- or 17-residue hemolytic peptides, some of which containing a D-amino acid in the second position of the sequence. The presence of this posttranslational modification confers the two isoforms distinctive biological properties, the D-amino acid–containing peptide being always more active than the corresponding L-isomer.
BOMBININS / Mangoni, Maria Luisa; Fiocco, Daniela; Barra, Donatella; Simmaco, Maurizio. - (2006), pp. 333-337.
BOMBININS
MANGONI, Maria Luisa;FIOCCO, Daniela;BARRA, Donatella;SIMMACO, Maurizio
2006
Abstract
The bombinin family of antimicrobial peptides is constituted by a number of molecules isolated from skin secretions of frogs belonging to the genus Bombina. These peptides can be grouped into two distinct subfamilies: the bombinin and the bombinin H. The former comprises 27-amino-acid residue peptides with antimicrobial activity against Gram-negative and Gram-positive bacteria and fungi; the latter includes 20- or 17-residue hemolytic peptides, some of which containing a D-amino acid in the second position of the sequence. The presence of this posttranslational modification confers the two isoforms distinctive biological properties, the D-amino acid–containing peptide being always more active than the corresponding L-isomer.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
