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Adsorption of Lysozyme on Silver and Its Influence on Silver Release
KTH, Skolan för kemivetenskap (CHE), Kemi, Yt- och korrosionsvetenskap.
KTH, Skolan för kemivetenskap (CHE), Kemi, Yt- och korrosionsvetenskap.ORCID-id: 0000-0002-2123-2201
KTH, Skolan för kemivetenskap (CHE), Kemi, Yt- och korrosionsvetenskap.ORCID-id: 0000-0003-2206-0082
KTH, Skolan för kemivetenskap (CHE), Kemi, Yt- och korrosionsvetenskap. SP Technical Research Institute of Swede.ORCID-id: 0000-0001-7496-1101
2014 (Engelska)Ingår i: Langmuir, ISSN 0743-7463, E-ISSN 1520-5827, Vol. 30, nr 46, s. 13877-13889Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

Silver is increasingly used in antimicrobial coatings of biomedical devices and implants to hinder infections. As proteins have been shown to largely influence the extent of released metals from various metal surfaces at biological conditions, silver may also be influenced in the same way. The aim of this study is to relate the structure of adsorbed lysozyme (LSZ) to the release of silver from metallic silver surfaces. Simultaneous adsorption measurements were performed in real time on the same surface using combined ellipsometry and quartz crystal microbalance with dissipation monitoring measurements to provide a more comprehensive understanding on the adsorption kinetics and the layer structures. The concentration of LSZ in 0.15 M NaNO3 solution (pH 7, 25 degrees C) influences the structure of the adsorbed layer. Monolayer coverage is obtained at concentrations =0.1 g/L, while a bilayer structure with a rigid inner layer and a relatively loosely adsorbed outer layer is formed at 1 g/L. The inner layer of LSZ is assumed to bind firmly to silver via disulfide bridges, which makes it irreversibly adsorbed with respect to dilution. The amount of released silver is further influenced by the structure of the LSZ layer. At low LSZ concentrations (=0.1 g/L) the amount of released silver is not significantly different compared with non-protein-containing NaNO3 solutions; however, noticeable reduction was observed at higher concentrations (1 g/L). This reduction in silver release has several possible explanations, including (i) surface complexation between LSZ and silver ions that may result in the incorporation of silver in the irreversible adsorbed layer and, hence, reduce the amount of released silver into solution, and (ii) net charge reversal at the protein/solution interface to slightly positive surface potentials. Any release of silver will therefore exhibit an electrostatic repulsion during transportation through the protein layer results in a reduced amount of silver in solution.

Ort, förlag, år, upplaga, sidor
2014. Vol. 30, nr 46, s. 13877-13889
Nyckelord [en]
Adsorption, Covalent bonds, Crystallography, Enzymes, Metal ions, Quartz, Adsorption kinetics, Adsorption measurement, Antimicrobial coatings, Biological conditions, Biomedical devices, Electrostatic repulsion, Quartz crystal microbalance with dissipation monitoring, Surface complexation
Nationell ämneskategori
Kemi Materialteknik
Identifikatorer
URN: urn:nbn:se:kth:diva-158285DOI: 10.1021/la503170xISI: 000345552000020PubMedID: 25363360Scopus ID: 2-s2.0-84912573332OAI: oai:DiVA.org:kth-158285DiVA, id: diva2:777873
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Vetenskapsrådet
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QC 20150109

Tillgänglig från: 2015-01-09 Skapad: 2015-01-07 Senast uppdaterad: 2017-12-05Bibliografiskt granskad

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Herting, GunillaOdnevall Wallinder, IngerBlomberg, Eva

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