期刊
JOURNAL OF PEPTIDE SCIENCE
卷 9, 期 11-12, 页码 679-689出版社
JOHN WILEY & SONS LTD
DOI: 10.1002/psc.500
关键词
amphiphilicity; antibiotics; conformation; lipopeptaibols; membranes; peptides; trichogin
Lipopeptaibols are members of a novel family of naturally occurring, short peptides with antimicrobial activity, characterized by a lipophilic acyl chain at the N-terminus, a high content of turn/helix inducing alpha-aminoisobutyric acid and a 1,2-amino alcohol at the C-terminus. Using solution methods, the prototypical lipopeptaibol trichogin GA IV and a large series of appropriately designed analogues were synthesized, which allow: (i) determination of the minimal lipid chain and peptide main-chain lengths for the onset of membrane activity, and (it) exploitation of a number of physico-chemical techniques aimed at assessing the trichogin preferred conformation under a variety of conditions and at investigating its mechanism of interaction with the phospholipid membranes. Copyright (C) 2003 European Peptide Society and John Wiley Sons, Ltd.
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