Testing human umbilical vein endothelial cells’ (HUVECs) response to functionalized lipid bilayer surfaces. The bilayer surfaces are prepared from peptide-amphiphiles using the Langmuir-Blodgett technique and are created to present a fibronectin-mimetic peptide at the exposed surface. The peptide-amphiphiles used are composed of 2 hydrocarbon tails, a short linker, the commonly-used adhesion amino acid sequence Arginine-Glycine-Aspartic Acid (RGD), a spacer mimicking both distance and hydrophilicy/hydrophobicity of the native protein, and finally the synergy site Proline-Histidine-Serine-Arginine-Asparagine (PHSRN). This peptide is a ligand targeting the α5β1 integrin expressed on the surface many cells, including endothelial cells. This ligand-integrin interaction is important in cell adhesion, which influences cell proliferation and migration, among other processes. Designing a peptide that can closely mimic fibronectin has far-reaching therapeutic effects for both interfacial interactions between biomaterials and the body, as well as targeted drug delivery.