Protein adsorption on hydroxyapatite nanosensors with different crystal sizes studied in situ by a quartz crystal microbalance with the dissipation method
Journal article, 2009

Hydroxyapatite (HAp) nanocrystals with different crystal sizes were deposited by the electrophoretic deposition method on the gold surface of a quartz crystal microbalance with a dissipation probe. The nanosensors formed this way were used to elucidate the adsorption mechanism of proteins with a similar pI value. The crystal sizes and the area of the a-plane affected only the adsorption amount of human serum albumin, but not that of bovine plasma fibrinogen. The viscoelastic property, Delta D/Delta f, of each absorbed layer on the nanosensors was almost constant. The protein adsorption mechanism can be explained as follows: the dissociated carboxyl groups (negative charge) of albumin were interacted with calcium ions and the hydrated amine groups (positive charge) at the alpha C domain of fibrinogen were with phosphate ions on the HAp surface.

spectroscopy

composite

vitro

serum

growth

ellipsometry

delivery

microparticles

liquid-chromatography

Surface-plasmon resonance

Author

T. Ikoma

National Institute for Materials Science

M. Tagaya

Tokyo Institute of Technology

National Institute for Materials Science

N. Hanagata

National Institute for Materials Science

Tomohiko Yoshioka

Tokyo Institute of Technology

Dinko Chakarov

Chalmers, Applied Physics, Chemical Physics

Bengt Herbert Kasemo

Chalmers, Applied Physics, Chemical Physics

J. Tanaka

Tokyo Institute of Technology

Journal of the American Ceramic Society

0002-7820 (ISSN)

Vol. 92 1125-1128

Subject Categories

Atom and Molecular Physics and Optics

DOI

10.1111/j.1551-2916.2009.02957.x