Engineered RGD Peptide Surface Regulates Adhesion, Spreading and Cytoskeletal Organization of Osteoblast-Like Cells

• Published in: Key Engineering Materials 2001-11, Vol.218-220, p.245-248
• Main Authors: Ducheyne, Paul, Composto, R.J., El-Ghannam, A., Shapiro, I.M.
• Format: Article
• Language: English
• ISSN: 1013-9826; 1662-9795; 1662-9795
• DOI: 10.4028/www.scientific.net/KEM.218-220.245

Bone cell adhesion at the surface of SiO2-based bioactive glasses is difficult to control since it depends on the adsorption of cell-adhesive proteins. Cell attachment activity is related to a tripeptide sequence, arginine-glycine-aspartic acid (RGD), located in the cell-binding domain of many adhesion molecules. Experiments are described showing that an RGD peptide can be linked to a silica surface through a 3-aminopropyl triethoxysilane (APTS) layer. Characterisation of the RGD surface showed that this treatment increased both the hydrophobicity and roughness of the surface. It is likely that the change in surface properties and the presence of bound RGD synergises integrin-mediated adherence of osteoblasts to the silica, resulting in reorganisation of the cytoskeleton. Thus, the grafted peptide profoundly modifies cell adhesion, spreading and cytodifferentiation. 6 refs.