Supported bilayers made of lipids and lipid-like amphiphiles have proven to be a very versatile platform for surface functionalization. Lipid bilayers that incorporate 'peptide amphiphiles' - peptides covalently linked to hydrocarbon tails - allow us to display peptides that can promote cell adhesion and proliferation on surfaces. In this contribution, we discuss the methods used to create these peptide displays and characterize them using a variety of surface analytical techniques including fluorescence microscopy and FRAP, AFM, and QCM. Our particular focus is on creating displays of multiple peptide ligands - e.g. GRGDSP paired with its synergy sequence PHSRN - wherein the relative composition and spatial presentation of these ligands can be tailored to optimize the cellular response. We also explore methods to cluster ligands on the nanoscale by using local phase separation in mixed-lipid bilayers to favor focal contact formation in adhering cells.