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https://hdl.handle.net/1822/42544
Título: | Polydopamine-mediated immobilization of alginate lyase to prevent P. aeruginosa adhesion |
Autor(es): | Alves, D. Sileika, Tadas Messersmith, Phillip Pereira, Maria Olívia |
Palavras-chave: | Funcionalization of polycarbonate surfaces with alginate lyase Dopamine-based coating strategy Antiadhesion surfaces Catalysis-independent performance alginate lyase antibacterial coating catalysis-independent dopamine chemistry |
Data: | Set-2016 |
Editora: | John Wiley and Sons |
Revista: | Macromolecular Bioscience |
Citação: | Alves, D.; Sileika, Tadas; Messersmith, Phillip; Pereira, Maria Olívia, Polydopamine-mediated immobilization of alginate lyase to prevent P. aeruginosa adhesion. Macromolecular Bioscience, 16(9), 1301-1310, 2016 |
Resumo(s): | Given alginate’s contribution to Pseudomonas aeruginosa virulence, it has long been considered a promising target for interventional therapies, which have been performed by using the enzyme alginate lyase. In this work, instead of treating pre-established mucoid biofi lms, alginate lyase is immobilized onto a surface as a preventive measure against P. aeruginosa adhesion. A polydopamine dip-coating strategy is employed for functionalization of polycarbonate surfaces. Enzyme immobilization is confi rmed by surface characterization. Surfaces functionalized with alginate lyase exhibit anti-adhesive properties, inhibiting the attachment of the mucoid strain. Moreover, surfaces modifi ed with this enzyme also inhibit the adhesion of the tested non-mucoid strain. Unexpectedly, treatment with heat-inactivated enzyme also inhibits the attachment of mucoid and non-mucoid P. aeruginosa strains. These fi ndings suggest that the antibacterial performance of alginate lyase functional coatings is catalysis-independent, highlighting the importance of further studies to better understand its mechanism of action against P. aeruginosa strains. |
Tipo: | Artigo |
URI: | https://hdl.handle.net/1822/42544 |
DOI: | 10.1002/mabi.201600077 |
ISSN: | 1616-5187 |
e-ISSN: | 1616-5195 |
Versão da editora: | http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1616-5195 |
Arbitragem científica: | yes |
Acesso: | Acesso aberto |
Aparece nas coleções: | CEB - Publicações em Revistas/Séries Internacionais / Publications in International Journals/Series |
Ficheiros deste registo:
Ficheiro | Descrição | Tamanho | Formato | |
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document_38954_1.pdf | 5,36 MB | Adobe PDF | Ver/Abrir |