López-Pérez, PM; Grimsey, E; Bourne, L; Mikut, R; Hilpert, K
(2017)
Screening and Optimizing Antimicrobial Peptides by Using SPOT-Synthesis.
Front Chem, 5.
p. 25.
https://doi.org/10.3389/fchem.2017.00025
SGUL Authors: Hilpert, Kai
Abstract
Peptide arrays on cellulose are a powerful tool to investigate peptide interactions with a number of different molecules, for examples antibodies, receptors or enzymes. Such peptide arrays can also be used to study interactions with whole cells. In this review, we focus on the interaction of small antimicrobial peptides with bacteria. Antimicrobial peptides (AMPs) can kill multidrug-resistant (MDR) human pathogenic bacteria and therefore could be next generation antibiotics targeting MDR bacteria. We describe the screen and the result of different optimization strategies of peptides cleaved from the membrane. In addition, screening of antibacterial activity of peptides that are tethered to the surface is discussed. Surface-active peptides can be used to protect surfaces from bacterial infections, for example implants.
Item Type: |
Article
|
Additional Information: |
Copyright © 2017 López-Pérez, Grimsey, Bourne, Mikut and Hilpert. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
Keywords: |
SPOT-synthesis, antimicrobial peptides, antimicrobial screening, multi-drug resistance, peptide libraries, peptide synthesis, substitution analysis, tethered peptides |
SGUL Research Institute / Research Centre: |
Academic Structure > Infection and Immunity Research Institute (INII) |
Journal or Publication Title: |
Front Chem |
Language: |
eng |
Dates: |
Date | Event |
---|
12 April 2017 | Published | 29 March 2017 | Accepted |
|
Publisher License: |
Creative Commons: Attribution 4.0 |
PubMed ID: |
28447030 |
![](http://static.pubmed.gov/portal/portal3rc.fcgi/2745237/img/27842) |
Go to PubMed abstract |
URI: |
https://openaccess.sgul.ac.uk/id/eprint/108814 |
Publisher's version: |
https://doi.org/10.3389/fchem.2017.00025 |
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