The detachment strength and morphology of bone cells contacting materials modified with a peptide sequence found within bone sialoprotein

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Abstract
Adhesion, spreading, and focal contact formation of primary bone‐derived cells on quartz surfaces grafted with a 15 amino acid peptide that contained a ‐RGD‐(‐Arg‐Gly‐Asp‐) sequence unique to bone sialoprotein was investigated. The peptide surfaces were fabricated by using a heterbifunctional crosslinker, sulfosuccinimidyal 4‐(N‐maleimidomethyl)cyclohexane‐1‐carboxylate, to link the peptide to amine functionalized quartz surfaces. Contact angle measurements, spectroscopic ellipsometry, and X‐ray photoelectron spectroscopy were used to confirm the chemistry and thickness of the overlayers. A radial flow apparatus was used to characterize cell detachment from peptide‐grafted surfaces. After 20 min of cell incubation, the strength of cell adhesion was significantly (p < 0.05) higher on the ‐RGD‐ compared to ‐RGE‐ (control) surfaces. Furthermore, the mean area of cells contacting the ‐RGD‐ was significantly (p < 0.05) higher than ‐RGE‐ surfaces. Vinculin staining showed formation of small focal contact patches on the periphery of bone cells incubated for 2 h on the ‐RGD‐ surfaces; however, few or no focal contacts were formed by cells seeded on the ‐RGE‐ grafted surfaces. The methods of peptide immobilization utilized in this study can be applied to implants, biosensors, and diagnostic devices that require specificity in cell adhesion. © 1997 John Wiley & Sons, Inc. J Biomed Mater Res, 37, 9–19, 1997.