Issue 77, 2016

Re-evaluation of the N-terminal substitution and the D-residues of teixobactin

Abstract

Teixobactin is a head to side-chain cyclic depsipeptide with a guanidino based residue within the cycle, three D-amino acids in the tail, and a N-methylated terminal residue. The synthesis of the first analogue, containing Arg, was recently described by our group. Herein, we demonstrated that analogues of Arg. Teixobactin bearing either (a) three L-amino acids in the tail and keeping the N-methyl at the N-terminal or (b) with three D-amino acids, but with acetylation of the N-terminal, are inactive against Gram(+) and Gram(−) bacteria. These results complement those published by the groups of Madder, Taylor, and Singh that have shown that both modifications: L-amino acids and N-acetylation also led to loss of biological activity.

Graphical abstract: Re-evaluation of the N-terminal substitution and the D-residues of teixobactin

Supplementary files

Article information

Article type
Communication
Submitted
11 jul 2016
Accepted
28 jul 2016
First published
28 jul 2016

RSC Adv., 2016,6, 73827-73829

Re-evaluation of the N-terminal substitution and the D-residues of teixobactin

S. A. H. Abdel Monaim, Y. E. Jad, G. A. Acosta, T. Naicker, E. J. Ramchuran, A. El-Faham, T. Govender, H. G. Kruger, B. G. de la Torre and F. Albericio, RSC Adv., 2016, 6, 73827 DOI: 10.1039/C6RA17720D

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.

Social activity

Spotlight

Advertisements