Tailoring the self-assembly of a tripeptide for the formation of antimicrobial surfaces

View/Open
Document typeArticle
Defense date2019-05-14
Rights accessOpen Access
Abstract
The accumulation of bacteria on surfaces is currently one of the greatest concerns f or the supply
of proper health, water
and energy. Here, we describe the mechanism by which a single peptide forms two
pH-dependent supramolecular particles that resist bacterial contamination. By using NMR and
molecular dynamics ( MD), we determined the structures of the peptide monomers and showed the
forces directing the self-assembly of each structure under different conditions. These peptide
assemblies change the characteristics of bare gla s and confer it with the ability to
prevent biofilm formation. Furthermore, they can adsorb and re ease active compounds as
demonstrated with an anticancer drug, antibiotic and enzyme. This synergism and the detailed
understanding of the proces ses are necessary for developing new sterile surfaces for health-care
systems, water puri ication devices, food packaging or any environment that suffers from
biocontamination.
CitationNir, S. [et al.]. Tailoring the self-assembly of a tripeptide for the formation of antimicrobial surfaces. "Nanoscale", 14 Maig 2019, núm. 18, p. 8752-8759.
ISSN2040-3364
Publisher versionhttps://pubs.rsc.org/en/content/articlelanding/2019/NR/C8NR10043H
Files | Description | Size | Format | View |
---|---|---|---|---|
Nir_et_all_nanoscale_2019.pdf | 566,4Kb | View/Open |
All rights reserved. This work is protected by the corresponding intellectual and industrial
property rights. Without prejudice to any existing legal exemptions, reproduction, distribution, public
communication or transformation of this work are prohibited without permission of the copyright holder