We have explored the use of poorly adhesive polymers covalently derivatized with cell adhesion peptides as routes to biomaterials which are adhesive to some types of cells but not adhesive to other types of cells. Cells adhere to synthetic biomaterials by interaction with adsorbed proteins of the cell adhesion molecule (CAM) family, including fibronectin, fibrinogen, vitronectin, and laminin, among others. Receptors for these proteins exist on the surfaces of cells, and it is through the interaction of these receptors with the adsorbed CAMs that adhesion is promoted. The most widely studied receptors are known as integrins (1) and are heterodimers of an α and a B subunit. Particular αB combinations confer varying degrees of specificity to the integrin. For example, the integrin αvB3, the classical vitronectin receptor, has broad specificity and binds to vitronectin, fibronectin, von Willebrand factor, osteopontin, and bone sialoprotein I. By contrast, the integrin α6B1 is much more narrowly specific and binds to only laminin. There are nonintegrin cell adhesion receptors as well, and one of the more important is a 67 KDa laminin receptor. The domains of the CAMs which bind to the receptors have been relatively well characterized in many cases (2). The prototypical binding domain is the tripeptide sequence arg-gly-asp-X (abbreviated in the single-letter nomenclature as RGDX). This sequence is found in many CAMs; for example, the sequence RGDS (S, ser) is active in fibronectin, fibrinogen, and von Willebrand factor; RGDV (V, val) in vitronectin; RGDT (T, thr) in collagen type I; and RGDN (N, asn) in laminin. Variations on the theme of RGD are also found, for example leu-asp-val (LDV) is active in some fibronectins, as is the sequence arg-glu-asp-val (REDV). Each of the above-specified sequences binds to one or more integrin receptors. Other sequences bind to nonintegrin receptors, such as the sequences tyr-ile-gly-ser-arg (YIGSR) and pro-asp-ser-gly-arg (PDSGR) of laminin.