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Surface Triggered Self-Assembly of Fmoc-Tripeptide as an Antibacterial Coating

In western countries, one patient on twenty will develop a nosocomial infection during his hospitalization at health care facilities. Classical antibiotics being less and less effective, this phenomenon is expanding year after year. Prevention of bacteria colonization of implantable medical devices...

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Autores principales: Criado-Gonzalez, Miryam, Iqbal, Muhammad Haseeb, Carvalho, Alain, Schmutz, Marc, Jierry, Loïc, Schaaf, Pierre, Boulmedais, Fouzia
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7438842/
https://www.ncbi.nlm.nih.gov/pubmed/32974302
http://dx.doi.org/10.3389/fbioe.2020.00938
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author Criado-Gonzalez, Miryam
Iqbal, Muhammad Haseeb
Carvalho, Alain
Schmutz, Marc
Jierry, Loïc
Schaaf, Pierre
Boulmedais, Fouzia
author_facet Criado-Gonzalez, Miryam
Iqbal, Muhammad Haseeb
Carvalho, Alain
Schmutz, Marc
Jierry, Loïc
Schaaf, Pierre
Boulmedais, Fouzia
author_sort Criado-Gonzalez, Miryam
collection PubMed
description In western countries, one patient on twenty will develop a nosocomial infection during his hospitalization at health care facilities. Classical antibiotics being less and less effective, this phenomenon is expanding year after year. Prevention of bacteria colonization of implantable medical devices constitutes a major medical and financial issue. In this study, we developed an antibacterial coating based on self-assembled Fmoc-tripeptide. Fmoc-FFpY peptides (F: phenylalanine; Y: tyrosine; p: PO(4)(2–)) are dephosphorylated enzymatically into Fmoc-FFY by action of alkaline phosphatase functionalized silica nanoparticles (NPs@AP), previously deposited on a surface. Fmoc-FFY peptides then self-assemble through π–π stacking interactions, hydrogen bonds and hydrophobic interactions adopting β-sheets secondary structures. The obtained hydrogel coatings show fibrillary structures observed by cryo-scanning electron microscopy with a thickness of few micrometers. At low concentration (≤0.5 mg.mL(–1)), self-assembled Fmoc-FFY has a superior antibacterial activity than Fmoc-FFpY peptide in solution. After 24 h of incubation, Fmoc-FFY hydrogel coatings fully inhibit the development of Gram-positive Staphylococcus aureus (S. aureus). The antibacterial effect is maintained on an in vitro model of repetitive infection in the case of S. aureus. This coating could serve in infections were Gram positive bacteria are prevalent, e.g., intravascular catheter infections. This work gives new insights toward the design of an alternative antimicrobial coating.
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spelling pubmed-74388422020-09-23 Surface Triggered Self-Assembly of Fmoc-Tripeptide as an Antibacterial Coating Criado-Gonzalez, Miryam Iqbal, Muhammad Haseeb Carvalho, Alain Schmutz, Marc Jierry, Loïc Schaaf, Pierre Boulmedais, Fouzia Front Bioeng Biotechnol Bioengineering and Biotechnology In western countries, one patient on twenty will develop a nosocomial infection during his hospitalization at health care facilities. Classical antibiotics being less and less effective, this phenomenon is expanding year after year. Prevention of bacteria colonization of implantable medical devices constitutes a major medical and financial issue. In this study, we developed an antibacterial coating based on self-assembled Fmoc-tripeptide. Fmoc-FFpY peptides (F: phenylalanine; Y: tyrosine; p: PO(4)(2–)) are dephosphorylated enzymatically into Fmoc-FFY by action of alkaline phosphatase functionalized silica nanoparticles (NPs@AP), previously deposited on a surface. Fmoc-FFY peptides then self-assemble through π–π stacking interactions, hydrogen bonds and hydrophobic interactions adopting β-sheets secondary structures. The obtained hydrogel coatings show fibrillary structures observed by cryo-scanning electron microscopy with a thickness of few micrometers. At low concentration (≤0.5 mg.mL(–1)), self-assembled Fmoc-FFY has a superior antibacterial activity than Fmoc-FFpY peptide in solution. After 24 h of incubation, Fmoc-FFY hydrogel coatings fully inhibit the development of Gram-positive Staphylococcus aureus (S. aureus). The antibacterial effect is maintained on an in vitro model of repetitive infection in the case of S. aureus. This coating could serve in infections were Gram positive bacteria are prevalent, e.g., intravascular catheter infections. This work gives new insights toward the design of an alternative antimicrobial coating. Frontiers Media S.A. 2020-08-07 /pmc/articles/PMC7438842/ /pubmed/32974302 http://dx.doi.org/10.3389/fbioe.2020.00938 Text en Copyright © 2020 Criado-Gonzalez, Iqbal, Carvalho, Schmutz, Jierry, Schaaf and Boulmedais. http://creativecommons.org/licenses/by/4.0/ 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) and the copyright owner(s) 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.
spellingShingle Bioengineering and Biotechnology
Criado-Gonzalez, Miryam
Iqbal, Muhammad Haseeb
Carvalho, Alain
Schmutz, Marc
Jierry, Loïc
Schaaf, Pierre
Boulmedais, Fouzia
Surface Triggered Self-Assembly of Fmoc-Tripeptide as an Antibacterial Coating
title Surface Triggered Self-Assembly of Fmoc-Tripeptide as an Antibacterial Coating
title_full Surface Triggered Self-Assembly of Fmoc-Tripeptide as an Antibacterial Coating
title_fullStr Surface Triggered Self-Assembly of Fmoc-Tripeptide as an Antibacterial Coating
title_full_unstemmed Surface Triggered Self-Assembly of Fmoc-Tripeptide as an Antibacterial Coating
title_short Surface Triggered Self-Assembly of Fmoc-Tripeptide as an Antibacterial Coating
title_sort surface triggered self-assembly of fmoc-tripeptide as an antibacterial coating
topic Bioengineering and Biotechnology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7438842/
https://www.ncbi.nlm.nih.gov/pubmed/32974302
http://dx.doi.org/10.3389/fbioe.2020.00938
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