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Adhesion of lactoferrin and bone morphogenetic protein-2 to a rutile surface: dependence on the surface hydrophobicity
Stockholm University, Faculty of Science, Department of Materials and Environmental Chemistry (MMK). Zhejiang University, People's Republic of China.
Stockholm University, Faculty of Science, Department of Materials and Environmental Chemistry (MMK).
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2014 (English)In: Biomaterials Science, ISSN 2047-4830, Vol. 2, no 8, 1090-1099 p.Article in journal (Refereed) Published
Abstract [en]

Binding of the proteins human lactoferrin (LF) and human bone morphogenetic protein-2 (BMP2) to a hydroxylated TiO2 rutile (110) surface has been modeled using molecular dynamics (MD) simulations. In order to study the effect of the hydrophobicity of the rutile surface on the protein binding process, the rutile surface was made more hydrophilic or more hydrophobic by adjusting the rutile atomic charges. The binding of LF and BMP2 to the hydrophobic rutile surface occurred through direct contact between the protein and rutile via both hydrophobic and hydrophilic amino acids. This forced the proteins to undergo structural rearrangements, observed primarily in BMP2. Binding to the hydrophilic rutile surface was largely indirect via the hydration layer of water on the surface of rutile. Both LF and BMP2 had a higher binding strength to the hydrophobic rutile surfaces than to the hydrophilic surfaces, as seen in the larger amplitude of the binding energies.

Place, publisher, year, edition, pages
2014. Vol. 2, no 8, 1090-1099 p.
National Category
Materials Chemistry
Research subject
Materials Chemistry
Identifiers
URN: urn:nbn:se:su:diva-106535DOI: 10.1039/c4bm00021hISI: 000338648500006OAI: oai:DiVA.org:su-106535DiVA: diva2:737069
Note

AuthorCount:5;

Available from: 2014-08-11 Created: 2014-08-11 Last updated: 2015-09-15Bibliographically approved

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Sun, TianyangHan, GuangShen, Zhijian
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