Abstract.
Lipopeptaibols are members of a novel group of naturally occurring, short peptides with antimicrobial activity, characterized by a lipophilic acyl chain at the N-terminus, a high content of the turn/helix forming α-aminoisobutyric acid and a 1,2-amino alcohol at the C-terminus. The amino acid sequences 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 residues. The longest peptides fold into a mixed 310/α helix, whereas the shortest peptides tend to adopt a β-turn/sheet structure. Using solution methodologies, a series of analogues of trichogin GA IV was synthesized which allowed determination of the minimal lipid chain and peptide main-chain lengths for the onset of membrane activity and exploitation of a number of spectroscopic techniques aimed at determining its preferred conformation under a variety of conditions and investigating in detail its mode of interaction with, and its effect on, the phospholipid membranes.
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Received 26 January 2001; received after revision 7 March 2001; accepted 15 March 2001
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Toniolo, C., Crisma, M., Formaggio, F. et al. Lipopeptaibols, a novel family of membrane active, antimicrobial peptides. CMLS, Cell. Mol. Life Sci. 58, 1179–1188 (2001). https://doi.org/10.1007/PL00000932
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DOI: https://doi.org/10.1007/PL00000932