Lipopeptaibols, a novel family of membrane active, antimicrobial peptides |
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Authors: | Toniolo C Crisma M Formaggio F Peggion C Epand R F Epand R M |
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Institution: | (1) Biopolymer Research Center, C.N.R., Department of Organic Chemistry, University of Padova, via Marzolo 1, 35131 Padova (Italy), Fax +39 049 827 5239, e-mail: biop02@chor.unipd.it , IT;(2) Department of Biochemistry, McMaster University, Health Sciences Centre, 1200 Main Street West, Hamilton, Ontario L8N 3Z5 (Canada), Fax +1 905 521 1397, e-mail: epand@mcmaster.ca , CA |
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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.
Received 26 January 2001; received after revision 7 March 2001; accepted 15 March 2001 |
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Keywords: | : Amino acid sequences amphiphilicity antibiotics membranes peptaibols peptides 3D-structure |
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