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Adsorption of Mefp-1: Influence of pH on adsorption kinetics and adsorbed amount
KTH Royal Institute of Technology, Sweden.
RISE., SP – Sveriges Tekniska Forskningsinstitut, SP Sveriges tekniska forskningsinstitut, YKI – Ytkemiska institutet. KTH Royal Institute of Technology, Sweden.
RISE., SP – Sveriges Tekniska Forskningsinstitut, SP Sveriges tekniska forskningsinstitut, YKI – Ytkemiska institutet. KTH Royal Institute of Technology, Sweden.
2012 (engelsk)Inngår i: Journal of Colloid and Interface Science, ISSN 0021-9797, E-ISSN 1095-7103, Vol. 379, nr 1, s. 107-113Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

Mussel adhesive proteins have received considerable attention due to their ability to bind strongly to many surfaces under water. Key structural features of these proteins include a large number of 3,4-dihydroxyphenyl-l-alanin (DOPA) and positively charged lysine residues. We elucidate the effects of solution pH, in the pH range 3-9, on adsorption kinetics, adsorbed amount, and layer structure on silicon oxynitride by employing Dual Polarization Interferometry. As a comparison, the cationic globular protein lysozyme was also investigated. The zeta-potential of the silicon oxynitride substrate was determined as a function of pH, and the isoelectric point was found to be below pH 3. Mefp-1 is positively charged at pH<10, and thus, the protein is expected to have an electrostatic attraction for the surface at all pH values investigated. The adsorbed amount and the initial adsorption rate were found to increase with solution pH, and no significant desorption occurred due to rinsing with pure water. The layer thickness after rinsing was 3-4nm, except at pH 3, where the adsorption was limited to a small amount. Covalent cross-linking of the Mefp-1 layer with NaIO 4 resulted in a small but significant compaction and increase in refractive index of the layer. The results are discussed in terms of the role of DOPA and electrostatic interactions for the adsorption of Mefp-1 to silicon oxynitride.

sted, utgiver, år, opplag, sider
2012. Vol. 379, nr 1, s. 107-113
Emneord [en]
Adsorption, Adsorption kinetics, Cross-linking, Dual Polarization Interferometry (DPI), Mefp-1, Mussel adhesive protein, Silicon oxynitride, Zeta-potential, Dual polarization interferometry, Mussel adhesive proteins, Silicon oxynitrides, Amino acids, Desorption, Kinetics, Laser beam effects, Proteins, Refractive index, Silicon nitride, Zeta potential, pH effects, lysozyme, Mytilus edulis foot protein 1, protein, silicon derivative, unclassified drug, water, accuracy, aqueous solution, article, chemical structure, cross linking, density, pH, priority journal, protein stability, surface charge, Hydrogen-Ion Concentration, Silicon Compounds, Solutions, Surface Properties
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Identifikatorer
URN: urn:nbn:se:ri:diva-51844DOI: 10.1016/j.jcis.2012.04.040Scopus ID: 2-s2.0-84861958400OAI: oai:DiVA.org:ri-51844DiVA, id: diva2:1516208
Merknad

Funding details: Stiftelsen för Strategisk Forskning, SSF; Funding text 1: This study was financially supported by MISTRA and the SSF Program “Microstructure, Corrosion and Friction Control,” Sweden, in collaboration with Biopolymer AB who supplied the Mefp-1. AD acknowledges a VINNMER fellowship from VINNOVA.

Tilgjengelig fra: 2021-01-11 Laget: 2021-01-11 Sist oppdatert: 2021-01-13bibliografisk kontrollert

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