Abstract
Adsorption of bovine serum albumin (BSA) and lysozyme (LSZ) proteins with preferred orientation to a(b)- and c-axes of single-crystal hydroxyapatite (HAp) particles, was investigated. Fiber-like HAp single crystal particles (aHAp) and plate-like HAp single crystal particles (cHAp) were used as models for a(b)-plane and c-plane oriented HAps, respectively, together with randomly shaped HAp particles (iHAp) as a control. The selective adsorption behaviors of negatively charged BSA and positively charged LSZ on these HAp particles were examined in a phosphate buffered saline at pH 7.3 and 25°C for 48h. The amount of BSA adsorption, normalized for specific surface area, was in the order of aHAp>iHAp>cHAp; however, the order for LSZ was reversed as cHAp>iHAp ≒ aHAp. These results indicate that the a(b)- and c-planes of HAp crystal have high specificity for the adsorption of acidic or basic proteins.
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