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Conformation and membrane activity of an analogue of the peptaibol antibiotic trichogin GA IV with a lipophilic amino acid at the N‐terminus
Author(s) -
Locardi Elsa,
Mammi Stefano,
Peggion Evaristo,
Monaco Vania,
Formaggio Fernando,
Crisma Marco,
Toniolo Claudio,
Bodo Bernard,
Rebuffat Sylvie,
Kamphuis Johan,
Broxterman Quirinus B.
Publication year - 1998
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/(sici)1099-1387(199809)4:6<389::aid-psc158>3.0.co;2-4
Subject(s) - moiety , chemistry , residue (chemistry) , peptide , stereochemistry , acetylation , membrane , side chain , amino acid , nuclear magnetic resonance spectroscopy , biochemistry , organic chemistry , gene , polymer
We have synthesized by solution‐phase methods two analogues of the 11‐residue lipopeptaibol antibiotic trichogin GA IV in which the N‐terminal n ‐octanoyl group is replaced either by an N‐acetylated 2‐amino‐2‐methyl‐ l ‐undecanoic acid or by an N‐acetylated α ‐aminoisobutyric acid. CD, FTIR absorption, and NMR analyses unequivocally show that the main structural features of trichogin GA IV are preserved in these analogues. Since only the peptide containing the lipophilic chain exhibits membrane‐modifying properties, these results strongly support the view that moving the long acyl moiety from the N α ‐blocking group to the side chain of the N‐terminal extra‐residue does not affect the conformational properties or the membrane activity of trichogin GA IV. © 1998 European Peptide Society and John Wiley & Sons, Ltd.