Adsorption of chondroitin-4-sulphate and heparin onto hydroxyapatite—effect of bovine serum albumin

The adsorption of chondroitin-4-sulphate (C4S) and heparin onto hydroxyapatite (HA) has been studied in the absence and presence of bovine serum albumin (BSA). Isotherm data at pH 6.8 have shown that BSA in solution has no effect on C4S adsorption, whereas heparin affinity and adsorption decrease. These data suggest that C4S and BSA bind to different calcium sites on the HA surface. Heparin and BSA may compete for the same calcium sites, or alternatively form heparin-BSA complexes leading to less binding due to steric effects. Evidence of an interaction between heparin and BSA in solution has been shown in this study, there being negligible interaction for C4S. BSA adsorption from solution onto HA decreases with increasing C4S/heparin solution concentration, which may be due to glycosaminoglycan-induced conformational change of BSA from a compact to an extended structure. For the HA precoated with BSA, both C4S and heparin adsorption decrease above a certain solution concentration. A possible explanation is that precoated BSA masks binding sites for the C4S/heparin. The percentage of BSA desorbed from the precoated HA in the presence of C4S and heparin is < 10% and < 30% respectively, indicating that BSA is strongly bound to the HA surface.