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Fibrinogen Adsorption on Hydroxyapatite, Carbonate Apatite andGold Surfaces In Situ Detected by Quartz CrystalMicrobalance with Resistance Technique

Published online by Cambridge University Press:  18 May 2012

Hiroshi Yonekura ,
Motohiro Tagaya ,
Tomohiko Yoshioka ,
Toshiyuki Ikoma  and
Junzo Tanaka
Hiroshi Yonekura
Affiliation:
Department of Metallurgy and Ceramics Science, Tokyo Institute of Technology, 2-12-1, Ookayama, Meguro-ku, Tokyo 152-8550, Japan
Motohiro Tagaya
Affiliation:
Department of Metallurgy and Ceramics Science, Tokyo Institute of Technology, 2-12-1, Ookayama, Meguro-ku, Tokyo 152-8550, Japan
Tomohiko Yoshioka
Affiliation:
Department of Metallurgy and Ceramics Science, Tokyo Institute of Technology, 2-12-1, Ookayama, Meguro-ku, Tokyo 152-8550, Japan
Toshiyuki Ikoma
Affiliation:
Department of Metallurgy and Ceramics Science, Tokyo Institute of Technology, 2-12-1, Ookayama, Meguro-ku, Tokyo 152-8550, Japan
Junzo Tanaka
Affiliation:
Department of Metallurgy and Ceramics Science, Tokyo Institute of Technology, 2-12-1, Ookayama, Meguro-ku, Tokyo 152-8550, Japan
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Abstract

When a biomaterial is implanted into the body, blood proteins adsorb on itssurface and subsequently cells adhere via the protein adlayer. Thus, theunderstanding of protein adsorption and conformational change on thebiomaterial surfaces is of great importance to control the biocompatibilitysuch as antithrombotic properties and cell adhesion behaviors. In thisstudy, we synthesized hydroxyapatite (HAp) and carbonate apatite (CAp) by awet method. Then we successfully fabricated the HAp and CAp sensors forQCM-R by an electrophoretic deposition method. Adsorption behavior ofproteins on the bone substitute material can be monitored by using theseapatite sensors. Bovine serum albumin and fibrinogen were employed for themodel proteins, and monitored the adsorption behavior on the HAp, CAp andreference gold (Au) sensors by the QCM-R technique. As a result, we revealedthat fibrinogen and bovine serum albumin adsorbs on the gold surface byhydrophobic interaction, and adsorbs on the HAp and CAp surfaces mainly byelectrostatic force. Besides, we revealed that fibrinogen adsorbs on the Ausurface more rigid than on the HAp and CAp surfaces while bovine serumalbumin adsorbs on the HAp and CAp surface more rigidly than on the Ausurface.

Keywords

biomaterialsurface chemistryCa

Information

Type
Research Article
Information
MRS Online Proceedings Library (OPL) , Volume 1418: Symposium LL/MM – Gels and Biomedical Materials , 2012 , mrsf11-1418-mm10-25
Copyright
Copyright © Materials Research Society 2012

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References

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