Conformation and membrane activity of an analogue of the peptaibol antibiotic trichogin GA IV with a lipophilic amino acid at the N-terminus
✍ Scribed by Elsa Locardi; Stefano Mammi; Evaristo Peggion; Vania Monaco; Fernando Formaggio; Marco Crisma; Claudio Toniolo; Bernard Bodo; Sylvie Rebuffat; Johan Kamphuis; Quirinus B. Broxterman
- Publisher
- John Wiley and Sons
- Year
- 1998
- Tongue
- English
- Weight
- 207 KB
- Volume
- 4
- Category
- Article
- ISSN
- 1075-2617
No coin nor oath required. For personal study only.
✦ Synopsis
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 h-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 h -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.