Molecular Modeling of Cell Adhesion Peptides on Hydroxyapatite and TiO2 Surfaces: Implication in Biomedical Implant Devices


Molecular modeling as a tool in studying peptide-substrate interactions provides insight on peptide adsorption conformation, adsorption energy, and stability of the peptide-inorganic interface. This work investigates the hydration and interaction of cell-adhesion peptides, specifically RGD and YIGSR, with the hydroxyapatite surface and TiO2 surface in cluster and periodic boundary condition approaches. The comparison of adsorption energies of RGD and YIGSR on both Hydroxyapatite (HA) and TiO2 surfaces reveals the similarities in adsorption energy and orientation pattern of peptides on both surfaces. The models demonstrate that initial peptide orientation affects adsorption energy for both. YIGSR is consistently more strongly adsorbed to HA-(001) surfaces and steps than RGD for both the surfaces. In addition, RGD maintained its “hairpin”-like structure during adsorption on a flat HA-(001) surface, and a slightly “relaxed hairpin” structure on TiO2 (110) surface. Adsorption energies of RGD on TiO2 (110) surface are significantly more favorable compared to HA-(001) surface, suggesting potential role of TiO2 as biomedical implants when tissue regeneration occurs via cell signaling.

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S. Biswas and U. Becker, "Molecular Modeling of Cell Adhesion Peptides on Hydroxyapatite and TiO2 Surfaces: Implication in Biomedical Implant Devices," Journal of Biomaterials and Nanobiotechnology, Vol. 4 No. 4, 2013, pp. 351-356. doi: 10.4236/jbnb.2013.44044.

Conflicts of Interest

The authors declare no conflicts of interest.


[1] M. Woo, J. Seo, R. Y. Zhang and P. X. Ma, “Suppression of Apoptosis by Enhanced Protein Adsorption on Polymer,” Biomaterials, Vol. 28, No. 16, 2007, pp. 2622-2630.
[2] S. P. Massia and J. A. Hubbell, “Covalent Surface Immobilization of Arg-Gly-Asp-and Tyr-Ile-Gly-Ser-Arg-Containing Peptides to Obtain Well-Defined Cell-Adhesive Substrates,” Analytical Biochemistry, Vol. 187, No. 2, 1990, pp. 292-301.
[3] Y. Iwamoto, F. A. Robey, J. Graf, M. Sasaki, H. K. Kleinman, Y. Yamada and G. R. Martin, “YIGSR, a Synthetic Lamininpentapeptide, Inhibits Experimental Metastasis Formation,” Science, Vol. 238, No. 4830, 1987, pp. 1132-1134.
[4] W. H. Kim, H. W. Schnaper, M. Nomizu, Y. Yamada and H. K. Kleinman, “Apoptosis in Human Fibrosarcoma Cells Is Induced by a Multimeric Synthetic Tyr-Ile-Gly-SerArg (YIGSR)-Containing Polypeptide from Laminin,” Cancer Research, Vol. 54, No. 18, 1994, pp. 5005-5010.
[5] E. Ruoslahti, “RGD and Other Recognition Sequences for Integrins,” Annual Review of Cell and Developmental Biology, Vol. 12, 1996, pp. 697-715.
[6] M. Kantlehner, D. Finsinger, J. Meyer, P. Schaffner, A. Jonczyk, B. Diefenbach, B. Nies and H. Kessler, “Selective RGD-Mediated Adhesion of Osteoblasts at Surfaces of Implants,” Angewandte Chemie International Edition, Vol. 38, No. 4, 1999, pp. 560-562.<560::AID-ANIE560>3.0.CO;2-F
[7] M. Gilbert, W. J. Shaw, J. R. Long, K. Nelson, G. P. Drobny, C. M. Giachelli and P. S. Stayton, “Chimeric Peptides of Statherin and Osteopontin That Bind Hydroxyapatite and Mediate Cell Adhesion,” Journal of Biological Chemistry, Vol. 275, No. 21, 2000, pp. 16213-16218.
[8] U. Becker, S. Biswas, T. Kendall, P. Risthaus, C. V. Putnis and C. M. Pina, “Interactions between Mineral Surfaces and Dissolved Species: From Monovalent Ions to Complex Organic Molecules,” American Journal of Science, Vol. 305, No. 6-8, 2005, pp. 791-825.
[9] C. Boiziau, S. Leroy, C. Reynaud, G. Lecayon, C. Legressus and P. Viel, “Elementary Mechanisms in the Interaction of Organic-Molecules with Mineral Surfaces,” Journal of Adhesion, Vol. 23, No. 1, 1987, pp. 21-44.
[10] A. Wierzbicki and H. S. Cheung, “Molecular Modeling of Inhibition of Hydroxyapatite by Phosphocitrate,” Journal of Molecular Structure: Theochem, Vol. 529, No. 1-3, 2000, pp. 73-82.
[11] N. H. de Leeuw, “A Computer Modeling Study of the Uptake and Segregation of Fluoride Ions at the Hydrated Hydroxyapatite (0001) Surface: Introducing a Ca10(PO4)6OH2 Potential Model,” Physical Chemistry Chemical Physics, Vol. 6, No. 8, 2004, pp. 1860-1866.
[12] D. Mkhonto and N. H. de Leeuw, “A Computer Modeling Study of the Effect of Water on the Surface Structure and Morphology of Fluorapatite: Introducing a Ca10(PO4)6F2 Potential Model,” Journal of Materials Chemistry, Vol. 12, No. 9, 2002, pp. 2633-2642.
[13] A. K. Rappe, C. J. Casewit, K. S. Colwell, W. A. Goddard and W. M. Skiff, “UFF, a Full Periodic-Table Force Field for Molecular-Mechanics and Molecular-Dynamics Simulations,” Journal of the American Chemical Society, Vol. 114, No. 25, 1992, pp. 10024-10035.
[14] J. D. Gale and A. L. Rohl, “The General Utility Lattice Program (GULP),” Molecular Simulation, Vol. 29, No. 5, 2003, pp. 291-341.
[15] A. K. Rappe and W. A. Goddard, “Charge Equilibration for Molecular-Dynamics Simulations,” Journal of Physical Chemistry, Vol. 95, No. 8, 1991, pp. 3358-3363.
[16] S. Biswas and U. Becker, “Molecular Modeling of Cell Adhesion Peptides on Hydroxyapatite Surfaces and Surface Steps: Application in Bone Tissue Engineering and Biomimetics,” 3rd International Conference on Chemical, Biological and Environment Sciences (ICCEBS’2013), Kuala Lumpur, 8-9 January 2013, pp. 59-63.
[17] L. Zhang and T. J. Webster, “Nanotechnology and Nanomaterials: Promises for Improved Tissue Regeneration,” Nano Today, Vol. 4, No. 1, 2009, pp. 66-80.
[18] M. J. Webber, J. A. Kessler and S. I. Stupp, “Emerging Peptide Nanomedicine to Regenerate Tissues and Organs,” Journal of Internal Medicine, Vol. 267, No. 1, 2010, pp. 71-88.

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