Introduction. Collagen has been used as a coating for titanium implants and as a bone tissue engineering scaffold material. The goal of this work was the characterisation of fibrils of collagen types I, II and III containing the following glycosaminoglycans (GAGs): chondroitin sulphates A, B and C (CSA,CSB,CSC), hyaluron and low and high molecular weight (MW) heparin and their influence in the form of coatings on human osteoblast (HO) behaviour. In addition, the effect of BMP-4 on HO behaviour was investigated. Methods. Fibrillogenesis took place at 37ºC in a 30 mM phosphate buffer at pH 7.4. GAG content of fibrils was measured colormetrically. Fibril morphology was studied by atomic force microscopy (AFM). Results and Discussion. Collagen type II fibrils bound more GAGs than fibrils of types I and III with the exception of hyaluron. GAGs were preferentially bound in the order CSC > high MW heparin > CSB > CSA > low MW heparin > hyaluron. Differences might be due to: a) differences in molecular weight; longer glycosaminoglycan chains may form more stable bonds with collagen by "bridging" more binding sites on collagen; b) different GAG charge densities; a higher charge density would lead to increased ionic binding. The amounts of GAG bound in this manner are comparable to those achieved by EDC/NHS crosslinking. HOs cultured on collagen-coated titanium surfaces containing CSA exhibited greater proliferation and collagen synthesis compared to those cultured on uncoated titanium. The addition of BMP-4 appeared to reduce proliferation and collagen synthesis, but seemed to stimulate the expression of osteoprotegerin and osteocalcin. Conclusions. The ability of collagen fibrils to bind GAGs varies according to GAG and collagen type. Coatings consisting of type I fibrils containing CSA and BMP-4 appear to modulate primary human osteoblast behaviour. These results may be of importance when designing collagen-based extra-cellular matrices.

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