Development of RGD peptides grafted onto silica surfaces: XPS characterization and human endothelial cell interactions

• Published in: Journal of biomedical materials research Vol. 46; no. 3; pp. 368 - 375
• Main Authors: Porté-Durrieu, M. C., Labrugère, C., Villars, F., Lefebvre, F., Dutoya, S., Guette, A., Bordenave, L., Baquey, C.
• Format: Journal Article
• Language: English
• Published: New York John Wiley & Sons, Inc 05-09-1999; John Wiley & Sons
• Subjects: Adhesion; Amino Acid Sequence; Amino acids; Biological and medical sciences; Biotechnology; Cell Adhesion; cell attachment; Cell Transplantation; Cells, Cultured; Cross-Linking Reagents; endothelial cell; Endothelium, Vascular - cytology; Fundamental and applied biological sciences. Psychology; grafting; Grafting (chemical); Humans; Immobilization of enzymes and other molecules; Immobilization techniques; Maleimides - chemistry; Methods. Procedures. Technologies; Molecular Sequence Data; Molecules; Oligopeptides; Organic compounds; Proteins; RGD; Silica; Silicon Dioxide - chemistry; Spectrometry, X-Ray Emission; Substrates; Surface Properties; Surfaces; Wettability; X ray photoelectron spectroscopy; XPS; Endothelial cell; Peptides; Contact interaction; Immobilization; Surface properties; Circulatory system; Technique; Silica; Umbilical vein
• ISSN: 0021-9304; 1097-4636
• DOI: 10.1002/(SICI)1097-4636(19990905)46:3<368::AID-JBM9>3.0.CO;2-8

The attachment of human umbilical vein endothelial cells (HUVECs) on substrates that had been covalently grafted with the cell adhesion peptides Arg‐Gly‐Asp (RGD) was investigated. This approach was used to provide substrates that are adhesive to cells even in the absence of serum proteins and to cells that have had no prior treatment of the surface with proteins that promote cell adhesion. We wanted to improve control of cellular interactions with cell‐adhesive materials by providing fixedly bound adhesion ligands. Silica was examined as a model surface. The peptides were grafted using three different steps: grafting of aminosilane molecules; reaction with a maleimide molecule; and immobilization of cell‐binding peptides containing the RGD sequence. The RGD‐grafted surface was characterized by X‐ray photoelectron spectroscopy (XPS) and contact‐angle measurements. © 1999 John Wiley & Sons, Inc. J Biomed Mater Res, 46, 368–375, 1999.