Issue 8, 2001

Short-chain analogues of the lipopeptaibol antibiotic trichogin GA IV: conformational analysis and membrane modifying properties

Abstract

To examine the role of the peptide main-chain length on the conformation and membrane activity of the lipopeptaibol antibiotic trichogin GA IV we have synthesized by solution methods the Leu11-OMe analogue and all its short, N-octanoylated C-terminal sequences. By FTIR absorption, 1H NMR and CD we have shown that largely folded, but not helical, forms characterize the short peptides, while the longest peptides predominantly adopt regular helical structures. Membrane activity is found in main-chain lengths as short as the tetrapeptide and progressively increases up to the undecapeptide.

Graphical abstract: Short-chain analogues of the lipopeptaibol antibiotic trichogin GA IV: conformational analysis and membrane modifying properties

Article information

Article type
Paper
Submitted
12 Feb 2001
Accepted
31 May 2001
First published
29 Jun 2001

J. Chem. Soc., Perkin Trans. 2, 2001, 1372-1377

Short-chain analogues of the lipopeptaibol antibiotic trichogin GA IV: conformational analysis and membrane modifying properties

F. Formaggio, C. Peggion, M. Crisma and C. Toniolo, J. Chem. Soc., Perkin Trans. 2, 2001, 1372 DOI: 10.1039/B101373O

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Spotlight

Advertisements