Next Article in Journal
Design, Synthesis, and Antitumor Activity of Novel Quinazoline Derivatives
Next Article in Special Issue
Antibacterial Synthetic Peptides Derived from Bovine Lactoferricin Exhibit Cytotoxic Effect against MDA-MB-468 and MDA-MB-231 Breast Cancer Cell Lines
Previous Article in Journal
Valorization of Lignin by Partial Wet Oxidation Using Sustainable Heteropoly Acid Catalysts
Article Menu
Issue 10 (October) cover image

Export Article

Open AccessCommunication
Molecules 2017, 22(10), 1632; doi:10.3390/molecules22101632

Investigation of the N-Terminus Amino Function of Arg10-Teixobactin

1
Catalysis and Peptide Research Unit, School of Health Sciences, University of KwaZulu-Natal, Durban 4001, South Africa
2
Department of Chemistry, College of Science, King Saud University, P.O. Box 2455, Riyadh 11451, Saudi Arabia
3
Chemistry Department, Faculty of Science, Alexandria University, P.O. Box 426, Ibrahimia, Alexandria 12321, Egypt
4
School of Chemistry and Physics, University of KwaZulu-Natal, Durban 4001, South Africa
5
Department of Organic Chemistry, University of Barcelona, Barcelona 08028, Spain
6
CIBER-BBN, Networking Centre on Bioengineering, Biomaterials and Nanomedicine, Barcelona Science Park, Barcelona 08028, Spain
7
KRISP, College of Health Sciences, University of KwaZulu-Natal, Durban 4001, South Africa
*
Authors to whom correspondence should be addressed.
Received: 28 August 2017 / Revised: 24 September 2017 / Accepted: 25 September 2017 / Published: 28 September 2017
(This article belongs to the Special Issue Peptide Therapeutics)
View Full-Text   |   Download PDF [712 KB, uploaded 29 September 2017]   |  

Abstract

Teixobactin is a recently described antimicrobial peptide that shows high activity against gram-positive bacteria as well as mycobacterium tuberculosis. Due to both its structure as a head-to-side chain cyclodepsipeptide and its activity, it has attracted the attention of several research groups. In this regard, a large number of analogs with substitutions in both the cycle and the tail has been described. Here, we report the contribution of the N-terminus residue, N-Me-d-Phe, to the activity of Arg10-teixobactin. On the basis of our findings, we conclude that the N-terminus accepts minimum changes but not the presence of long alkyl chains. The presence of a positive charge is a requirement for the activity of the peptide. Furthermore, acylation of the N-terminus leads to total loss of activity. View Full-Text
Keywords: antimicrobial peptides; teixobactin; lipophilicity; solid-phase peptide synthesis; cyclic depsipeptides antimicrobial peptides; teixobactin; lipophilicity; solid-phase peptide synthesis; cyclic depsipeptides
Figures

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Supplementary material

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Monaim, S.A.H.A.; Noki, S.; Ramchuran, E.J.; El-Faham, A.; Albericio, F.; Torre, B.G. Investigation of the N-Terminus Amino Function of Arg10-Teixobactin. Molecules 2017, 22, 1632.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]

Molecules EISSN 1420-3049 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top