Dissolution/reprecipitation and protein adsorption studies of calcium phosphate coatings by FT-IR/ATR techniques
✍ Scribed by Ong, J. L. ;Chittur, K. K. ;Lucas, L. C.
- Publisher
- John Wiley and Sons
- Year
- 1994
- Tongue
- English
- Weight
- 999 KB
- Volume
- 28
- Category
- Article
- ISSN
- 0021-9304
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✦ Synopsis
Abstract
The surfaces of bioactive Ca‐P ceramics immediately change when exposed to proteinaceous solutions. The dissolution behavior and protein interactions of these bioactive materials at the bone/implant interface need to be investigated to understand their material‐cellular interactions fully. In this study, FT‐IR/ATR techniques were used to study the in situ phosphate release kinetics of Ca‐P coatings. The net loss of phosphate molecules from coatings was slower in saline solutions compared with α‐MEM solutions. Coatings exposed to α‐MEM solutions containing fibronectin released phosphate molecules slower than coatings exposed to α‐MEM solutions containing albumin. Conformational changes in fibronectin and albumin adsorbed onto Ca‐P and uncoated germanium surfaces were also investigated using FT‐IR/ATR spectroscopy. Analysis of changes in the amide I bands indicated that there was a greater loss of β‐sheet structure in adsorbed fibronectin on Ca‐P coatings when compared with bare germanium surfaces. Although albumin did change its structure upon adsorption on both Ca‐P and germanium, unlike fibronectin, adsorbed albumin structure was similar on Ca‐P coatings and germanium. Furthermore, with time the conformation of adsorbed fibronectin and albumin appeared to be very stable on Ca‐P coatings, whereas albumin adsorbed to germanium exhibited an increase in ratio of α‐helix to βturn. © 1994 John Wiley & Sons, Inc.