Lipopeptaibols, a novel family of membrane active, antimicrobial peptides

Citation
C. Toniolo et al., Lipopeptaibols, a novel family of membrane active, antimicrobial peptides, CELL MOL L, 58(9), 2001, pp. 1179-1188
Citations number
61
Language
INGLESE
art.tipo
Review
Categorie Soggetti
Cell & Developmental Biology
Journal title
CELLULAR AND MOLECULAR LIFE SCIENCES
ISSN journal
1420-682X → ACNP
Volume
58
Issue
9
Year of publication
2001
Pages
1179 - 1188
Database
ISI
SICI code
1420-682X(200108)58:9<1179:LANFOM>2.0.ZU;2-C
Abstract
Lipopeptaibols are members of a novel group of naturally occurring, short p eptides with antimicrobial activity, characterized by a lipophilic acyl cha in at the N-terminus, a high content of the turn/helix forming alpha -amino isobutyric acid and a 1,2-amino alcohol at the C-terminus. The amino acid s equences range from 6 to 10 residues and the fatty acyl moieties from 8 to 15 carbon atoms. The peptide portion of lipopeptaibols can be shorter than those of the nonlipidated peptaibols that range from 10 to 19 amino acid re sidues. The longest peptides fold into a mixed 3(10)/alpha helix, whereas t he shortest peptides tend to adopt a beta -turn/sheet structure. Using solu tion methodologies, a series of analogues of trichogin GA IV was synthesize d which allowed determination of the minimal lipid chain and peptide main-c hain lengths for the onset of membrane activity and exploitation of a numbe r of spectroscopic techniques aimed at determining its preferred conformati on under a variety of conditions and investigating in detail its mode of in teraction with, and its effect on, the phospholipid membranes.