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Surface modification of Ti45Nb alloy by immobilization of RGD peptide via self assembled monolayer

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Abstract

A new low modulus β Ti-Nb alloy with low elastic modulus and excellent corrosion resistance is currently under consideration as a surgical implant material. The usefulness of such materials can be dramatically enhanced if their surface structure and surface chemistry can be controlled. This control is achieved by attaching a self assembled monolayer (SAM) based on 11-chloroacetyl-1-undecylphosphonic acid, CAUDPA, to the surface and immobilization of a peptide to the monolayer. The SAM is characterized by Fourier Transform Infrared Spectroscopy (FTIR) and X-ray Photoelectron Spectroscopy (XPS) at two different takeoff angles. The CAUDPA molecules were covalently bonded on the substrate in a configuration in which the phosphonic group turns toward the Ti45Nb while the acetyl chloride end group tail turns to the topmost surface. In such configuration sequential in situ reaction is possible by exchange between the chloride and a biological molecule. Such biological molecule is the arginine-glycine-aspartic acid-cysteine, RGDC, small amino acid sequence present in many molecules of the extracellular matrix. Preliminary cell culture in-vitro result shows an improvement of the response of osteoblast cells to Ti45Nb after the peptide immobilization.

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Acknowledgments

The authors want to thank Dr. Reuven Brener from the Solid State Institute, Technion for his assistance in XPS analyses, and Dr. Anna Weiss from the Medical Faculty, Technion for cell culture preparation. We acknowledge the financial support of G.I.F. Research Grant N0 I-810-236.10/200, Commission of the European Communities, Network of Excellence EXCELL and of the Minerva Center for Tailored Biomaterial Interfaces at Bar Ilan University.

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Correspondence to I. Gotman.

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Zorn, G., Gotman, I., Gutmanas, E.Y. et al. Surface modification of Ti45Nb alloy by immobilization of RGD peptide via self assembled monolayer. J Mater Sci: Mater Med 18, 1309–1315 (2007). https://doi.org/10.1007/s10856-006-0117-7

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  • DOI: https://doi.org/10.1007/s10856-006-0117-7

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