title: Polydopamine-Mediated Immobilization of Alginate Lyase to Prevent P. aeruginosa Adhesion.
abstract: 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 biofilms, 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 confirmed by surface characterization. Surfaces functionalized with alginate lyase exhibit anti-adhesive properties, inhibiting the attachment of the mucoid strain. Moreover, surfaces modified 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 findings 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.
authors.affiliation: CEB - Centre of Biological Engineering, LIBRO - Laboratório de Investigação em Biofilmes Rosário Oliveira, University of Minho, Campus de Gualtar, 4710-057, Braga, Portugal. dianalves@ceb.uminho.pt.
authors.forename: Diana
authors.initials: D
authors.lastname: Alves
authors.affiliation: Biomedical Engineering Department, Northwestern University, 2145 Sheridan Road, Evanston, IL, 60208, USA.
authors.forename: Tadas
authors.initials: T
authors.lastname: Sileika
authors.affiliation: Biomedical Engineering Department, Northwestern University, 2145 Sheridan Road, Evanston, IL, 60208, USA.|Department of Bioengineering and Department of Materials Science and Engineering, University of California, Berkeley, CA, 94720-1760, USA.
authors.forename: Phillip B
authors.initials: PB
authors.lastname: Messersmith
authors.affiliation: CEB - Centre of Biological Engineering, LIBRO - Laboratório de Investigação em Biofilmes Rosário Oliveira, University of Minho, Campus de Gualtar, 4710-057, Braga, Portugal. mopereira@deb.uminho.pt.
authors.forename: Maria Olívia
authors.initials: MO
authors.lastname: Pereira
mesh_terms: D000900:Anti-Bacterial Agents / Q000494:pharmacology; D001422:Bacterial Adhesion / Q000187:drug effects*; D004800:Enzymes, Immobilized / Q000378:metabolism*; D005453:Fluorescence; D007211:Indoles / Q000494:pharmacology*; D050296:Microbial Viability / Q000187:drug effects; D056951:Photoelectron Spectroscopy; D011108:Polymers / Q000494:pharmacology*; D011133:Polysaccharide-Lyases / Q000378:metabolism*; D011550:Pseudomonas aeruginosa / Q000187:drug effects / Q000502:physiology*
chemical_list: D000900:Anti-Bacterial Agents; D004800:Enzymes, Immobilized; D007211:Indoles; D011108:Polymers; C568283:polydopamine; D011133:Polysaccharide-Lyases; C016158:poly(beta-D-mannuronate) lyase
keywords: alginate lyase; antibacterial coating; catalysis-independent; dopamine chemistry