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

被引：61
作者：
Mangoni, ML
Grovale, N
Giorgi, A
Mignogna, G
Simmaco, M
Barra, D
机构：
[1] Univ Roma La Sapienza, Dipartimento Sci Biochim A Rossi Fanelli, I-00185 Rome, Italy
[2] Univ Roma La Sapienza, CNR, Ctr Mol Biol, I-00185 Rome, Italy
[3] Univ G DAnnunzio, Dipartimento Sci Biomed, I-66100 Chieti, Italy
来源：
PEPTIDES | 2000年 / 21卷 / 11期
关键词：
antimicrobial peptides; bombinin H; D-amino acid; amphibia; Bombina genus;
D O I：
10.1016/S0196-9781(00)00316-8
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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-1(D)/GH-1(L), 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. (C) 2000 Elsevier Science Inc. All rights reserved.
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收藏
页码：1673 / 1679
页数：7
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