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Rapid Assembly of Infection-Resistant Coatings: Screening and Identification of Antimicrobial Peptides Works in Cooperation with an Antifouling Background.

Yu, K; Alzahrani, A; Khoddami, S; Cheng, JTJ; Mei, Y; Gill, A; Luo, HD; Haney, EF; Hilpert, K; Hancock, REW; et al. Yu, K; Alzahrani, A; Khoddami, S; Cheng, JTJ; Mei, Y; Gill, A; Luo, HD; Haney, EF; Hilpert, K; Hancock, REW; Lange, D; Kizhakkedathu, JN (2021) Rapid Assembly of Infection-Resistant Coatings: Screening and Identification of Antimicrobial Peptides Works in Cooperation with an Antifouling Background. ACS Appl Mater Interfaces, 13 (31). pp. 36784-36799. ISSN 1944-8252 https://doi.org/10.1021/acsami.1c07515
SGUL Authors: Hilpert, Kai

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Abstract

Bacterial adhesion and the succeeding biofilm formation onto surfaces are responsible for implant- and device-associated infections. Bifunctional coatings integrating both nonfouling components and antimicrobial peptides (AMPs) are a promising approach to develop potent antibiofilm coatings. However, the current approaches and chemistry for such coatings are time-consuming and dependent on substrates and involve a multistep process. Also, the information is limited on the influence of the coating structure or its components on the antibiofilm activity of such AMP-based coatings. Here, we report a new strategy to rapidly assemble a stable, potent, and substrate-independent AMP-based antibiofilm coating in a nonfouling background. The coating structure allowed for the screening of AMPs in a relevant nonfouling background to identify optimal peptide combinations that work in cooperation to generate potent antibiofilm activity. The structure of the coating was changed by altering the organization of the hydrophilic polymer chains within the coatings. The coatings were thoroughly characterized using various surface analytical techniques and correlated with the efficiency to prevent biofilm formation against diverse bacteria. The coating method that allowed the conjugation of AMPs without altering the steric protection ability of hydrophilic polymer structure results in a bifunctional surface coating with excellent antibiofilm activity. In contrast, the conjugation of AMPs directly to the hydrophilic polymer chains resulted in a surface with poor antibiofilm activity and increased adhesion of bacteria. Using this coating approach, we further established a new screening method and identified a set of potent surface-tethered AMPs with high activity. The success of this new peptide screening and coating method is demonstrated using a clinically relevant mouse infection model to prevent catheter-associated urinary tract infection (CAUTI).

Item Type: Article
Additional Information: This document is the Accepted Manuscript version of a Published Work that appeared in final form in ACS Applied Materials and Interfaces, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see https://doi.org/10.1021/acsami.1c07515
Keywords: antibiofilm coating, antimicrobial peptides, bifunctional coating, implant-associated infection, screening method, substrate-independent coating, antibiofilm coating, antimicrobial peptides, bifunctional coating, implant-associated infection, screening method, substrate-independent coating, 0904 Chemical Engineering, 0303 Macromolecular and Materials Chemistry, 0306 Physical Chemistry (incl. Structural), Nanoscience & Nanotechnology
SGUL Research Institute / Research Centre: Academic Structure > Infection and Immunity Research Institute (INII)
Journal or Publication Title: ACS Appl Mater Interfaces
ISSN: 1944-8252
Language: eng
Dates:
DateEvent
11 August 2021Published
30 July 2021Published Online
1 July 2021Accepted
Publisher License: Publisher's own licence
Projects:
Project IDFunderFunder ID
UNSPECIFIEDNatural Science and Engineering Research Council of CanadaUNSPECIFIED
FDN-154287Canadian Institutes of Health Researchhttp://dx.doi.org/10.13039/501100000024
UNSPECIFIEDMichael Smith Foundation for Health Researchhttp://dx.doi.org/10.13039/501100000245
PubMed ID: 34328312
Go to PubMed abstract
URI: https://openaccess.sgul.ac.uk/id/eprint/113526
Publisher's version: https://doi.org/10.1021/acsami.1c07515

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