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In an effort to regulate mammalian cell behavior in contact with solid material surfaces, we have functionalized surfaces with different ratios of both the putative cell binding (‐Arg‐Gly‐Asp‐) domain and a consensus heparan‐binding domain. The peptide sequences ‐Arg‐Gly‐Asp‐ (‐RGD‐) and ‐Phe‐His‐Arg‐Arg‐Ile‐Lys‐Ala‐ (‐FHRRIKA‐) or mixtures of the two in the ratios of 75:25 (mimetic peptide surface I), 25:75 (mimetic peptide surface II), and 50:50 (mimetic peptide surface III) were immobilized on model surfaces using a heterobifunctional cross‐linker to link the peptide(s) to amine‐functionalized quartz surfaces. Contact angle measurements, spectroscopic ellipsometry, and X‐ray photoelectron spectroscopy were used to confirm the chemistry, thickness of the overlayers, and surface density of immobilized peptides (∼4−6 pmol/cm²). The degree of rat calvaria osteoblast‐like cell spreading, focal contact …