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

Toshiyuki Ikoma ; Motohiro Tagaya ; Nobutaka Hanagata ; Tomohiko Yoshioka ; Dinko Chakarov (Institutionen för teknisk fysik, Kemisk fysik) ; Bengt Kasemo (Institutionen för teknisk fysik, Kemisk fysik) ; Junzo Tanaka
Journal of the American Ceramic Society (0002-7820). Vol. 92 (2009), 5, p. 1125-1128.
[Artikel, refereegranskad vetenskaplig]

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.

Nyckelord: Surface-plasmon resonance, liquid-chromatography, composite, vitro, microparticles, ellipsometry, spectroscopy, delivery, growth, serum



Denna post skapades 2010-01-26. Senast ändrad 2013-10-29.
CPL Pubid: 110944

 

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Institutioner (Chalmers)

Institutionen för teknisk fysik, Kemisk fysik (1900-2015)

Ämnesområden

Kemisk fysik

Chalmers infrastruktur