Novel dialkyl chain amphiphiles containing peptides derived from extracellular matrix collagen ligand sequences have been synthesized using a highly efficient solid-phase approach. These compounds have been shown to form stable monolayers at the air-water interface. Monolayer features are determined by the peptide head group and are dependent on the peptide sequence. The peptide packing implied by the head group area is denser than the packing of a fully hydrated random coil structure. At high surface pressures, peptide amphiphiles can be compressed to molecular areas corresponding to fully extended peptide chains. The interfacial monolayer behavior of the peptide amphiphiles is compared to that of a series of novel compounds containing various amino acids in their head group region. Monolayers of these compounds permit investigation of model membranes containing the functional elements of proteins such as those involved in cell adhesion and signaling.