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On the mechanism of protein adsorption onto hydroxylated and nonhydroxylated TiO2 surfaces
Royal Inst Technol, Sch Biotechnol, Dept Theoret Chem, S-10691 Stockholm, Sweden; Zhejiang Univ, Dept Chem, Hangzhou 310027, Zhejiang, Peoples R China.
Royal Inst Technol, Sch Biotechnol, Dept Theoret Chem, S-10691 Stockholm, Sweden.
Örebro University, School of Science and Technology.
Zhejiang Univ, Dept Chem, Hangzhou 310027, Zhejiang, Peoples R China.
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2010 (English)In: The Journal of Physical Chemistry C, ISSN 1932-7447, E-ISSN 1932-7455, Vol. 114, no 34, p. 14496-14502Article in journal (Refereed) Published
Abstract [en]

Protein adsorption onto implant surfaces is of great importance for the regulation of implant bioactivity. Surface modification of implants is a promising way in the molecular design of biocompatible materials against nonspecific adsorption of proteins. On the basis of these fundamental facts, we focus in this work on the different behavior of protein adsorption on hydroxylated and nonhydroxylated rutile TiO2 (110) surfaces through molecular dynamics simulations. Our investigation indicates that the distribution of the water molecules at the interface induced by the surface modification plays an important role in the protein adsorption. The surface with modified hydroxyl groups was observed to have much greater affinity to the protein, as reflected by the larger protein−surface electrostatic interaction and by the larger amount of adsorbed residues. The highly ordered structure of the modified hydroxyl groups on the hydroxylated surface diminishes the possibility of hydrogen bond formation between the surface and the water molecules above it, which in turn makes it easier for the protein to move closer to the surface with hydroxyl modification.

Place, publisher, year, edition, pages
Washington DC, USA: American Chemical Society (ACS), 2010. Vol. 114, no 34, p. 14496-14502
National Category
Chemical Sciences
Research subject
Chemistry
Identifiers
URN: urn:nbn:se:oru:diva-12634DOI: 10.1021/jp1037156ISI: 000281129100026Scopus ID: 2-s2.0-77956149715OAI: oai:DiVA.org:oru-12634DiVA: diva2:373771
Available from: 2010-12-01 Created: 2010-12-01 Last updated: 2017-12-12Bibliographically approved

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Tu, Yaoquan

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