Protein-Engineered Polymers Functionalized with Antimicrobial Peptides for the Development of Active Surfaces

Antibacterial resistance is a major worldwide threat due to the increasing number of infections caused by antibiotic-resistant bacteria with medical devices being a major source of these infections. This suggests the need for new antimicrobial biomaterial designs able to withstand the increasing pre...

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Main Authors: Ana Margarida Pereira, Diana Gomes, André da Costa, Simoni Campos Dias, Margarida Casal, Raul Machado
Format: Article
Language:English
Published: MDPI AG 2021-06-01
Series:Applied Sciences
Subjects:
Online Access:https://www.mdpi.com/2076-3417/11/12/5352
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spelling doaj-2fa7e078025e4e189083b1b451755d362021-06-30T23:42:46ZengMDPI AGApplied Sciences2076-34172021-06-01115352535210.3390/app11125352Protein-Engineered Polymers Functionalized with Antimicrobial Peptides for the Development of Active SurfacesAna Margarida Pereira0Diana Gomes1André da Costa2Simoni Campos Dias3Margarida Casal4Raul Machado5CBMA (Centre of Molecular and Environmental Biology), Department of Biology, Campus de Gualtar, University of Minho, 4710-057 Braga, PortugalCBMA (Centre of Molecular and Environmental Biology), Department of Biology, Campus de Gualtar, University of Minho, 4710-057 Braga, PortugalCBMA (Centre of Molecular and Environmental Biology), Department of Biology, Campus de Gualtar, University of Minho, 4710-057 Braga, PortugalGenomic Sciences and Biotechnology Program, UCB-Brasilia, SgAN 916, Modulo B, Bloco C, Brasília 70790-160, BrazilCBMA (Centre of Molecular and Environmental Biology), Department of Biology, Campus de Gualtar, University of Minho, 4710-057 Braga, PortugalCBMA (Centre of Molecular and Environmental Biology), Department of Biology, Campus de Gualtar, University of Minho, 4710-057 Braga, PortugalAntibacterial resistance is a major worldwide threat due to the increasing number of infections caused by antibiotic-resistant bacteria with medical devices being a major source of these infections. This suggests the need for new antimicrobial biomaterial designs able to withstand the increasing pressure of antimicrobial resistance. Recombinant protein polymers (rPPs) are an emerging class of nature-inspired biopolymers with unique chemical, physical and biological properties. These polymers can be functionalized with antimicrobial molecules utilizing recombinant DNA technology and then produced in microbial cell factories. In this work, we report the functionalization of rPBPs based on elastin and silk-elastin with different antimicrobial peptides (AMPs). These polymers were produced in <i>Escherichia coli</i>, successfully purified by employing non-chromatographic processes, and used for the production of free-standing films. The antimicrobial activity of the materials was evaluated against Gram-positive and Gram-negative bacteria, and results showed that the polymers demonstrated antimicrobial activity, pointing out the potential of these biopolymers for the development of new advanced antimicrobial materials.https://www.mdpi.com/2076-3417/11/12/5352antimicrobial resistanceantimicrobial surfacesantimicrobial filmsrecombinant protein polymerssilk-elastin proteinselastin-like recombinamers
collection DOAJ
language English
format Article
sources DOAJ
author Ana Margarida Pereira
Diana Gomes
André da Costa
Simoni Campos Dias
Margarida Casal
Raul Machado
spellingShingle Ana Margarida Pereira
Diana Gomes
André da Costa
Simoni Campos Dias
Margarida Casal
Raul Machado
Protein-Engineered Polymers Functionalized with Antimicrobial Peptides for the Development of Active Surfaces
Applied Sciences
antimicrobial resistance
antimicrobial surfaces
antimicrobial films
recombinant protein polymers
silk-elastin proteins
elastin-like recombinamers
author_facet Ana Margarida Pereira
Diana Gomes
André da Costa
Simoni Campos Dias
Margarida Casal
Raul Machado
author_sort Ana Margarida Pereira
title Protein-Engineered Polymers Functionalized with Antimicrobial Peptides for the Development of Active Surfaces
title_short Protein-Engineered Polymers Functionalized with Antimicrobial Peptides for the Development of Active Surfaces
title_full Protein-Engineered Polymers Functionalized with Antimicrobial Peptides for the Development of Active Surfaces
title_fullStr Protein-Engineered Polymers Functionalized with Antimicrobial Peptides for the Development of Active Surfaces
title_full_unstemmed Protein-Engineered Polymers Functionalized with Antimicrobial Peptides for the Development of Active Surfaces
title_sort protein-engineered polymers functionalized with antimicrobial peptides for the development of active surfaces
publisher MDPI AG
series Applied Sciences
issn 2076-3417
publishDate 2021-06-01
description Antibacterial resistance is a major worldwide threat due to the increasing number of infections caused by antibiotic-resistant bacteria with medical devices being a major source of these infections. This suggests the need for new antimicrobial biomaterial designs able to withstand the increasing pressure of antimicrobial resistance. Recombinant protein polymers (rPPs) are an emerging class of nature-inspired biopolymers with unique chemical, physical and biological properties. These polymers can be functionalized with antimicrobial molecules utilizing recombinant DNA technology and then produced in microbial cell factories. In this work, we report the functionalization of rPBPs based on elastin and silk-elastin with different antimicrobial peptides (AMPs). These polymers were produced in <i>Escherichia coli</i>, successfully purified by employing non-chromatographic processes, and used for the production of free-standing films. The antimicrobial activity of the materials was evaluated against Gram-positive and Gram-negative bacteria, and results showed that the polymers demonstrated antimicrobial activity, pointing out the potential of these biopolymers for the development of new advanced antimicrobial materials.
topic antimicrobial resistance
antimicrobial surfaces
antimicrobial films
recombinant protein polymers
silk-elastin proteins
elastin-like recombinamers
url https://www.mdpi.com/2076-3417/11/12/5352
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