Adsorption of chondroitin-4-sulphate and heparin onto titanium: effect of bovine serum albumin

The adsorption of chondroitin-4-sulphate (C4S) and heparin onto titanium has been studied in the absence and presence of bovine serum albumin (BSA). Isotherm data (0.02 image calcium acetate, pH 6.8) have shown that BSA in solution and BSA-coated titanium result in decreased adsorption for both C4S and heparin. For the BSA in solution data, C4S/heparin and BSA may compete for the same sites on the titanium surface via calcium ions, or alternatively in the case of heparin, complexes of heparin and BSA form in solution, 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 between C4S and BSA. BSA adsorption from solution investigated in the presence of C4S/heparin decreases with increasing C4S/heparin solution concentration. This may be due to a glycosaminoglycan (GAG) induced conformational change of BSA from a compact to an extended structure. The decreased adsorption onto BSA-coated titanium may be due to masking of the GAG binding sites, this effect being greater for C4S. Desorption of BSA from the pre-coated titanium in the presence of C4S and heparin is <10% and <30% respectively, indicating that BSA is strongly bound to the titanium surface.