SYNTHETIC LIPIDATION OF PEPTIDES AND AMINO-ACIDS - MONOLAYER STRUCTURE AND PROPERTIES

Novel dialkyl chain amphiphiles containing peptides derived from extra cellular matrix collagen ligand sequences have been synthesized using a highly efficient solid-phase approach. These compounds have been sho wn to form stable monolayers at the air-water interface. Monolayer fea tures are determined by the peptide head group and are dependent on th e 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 m olecular areas corresponding to fully extended peptide chains. The int erfacial 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 investig ation of model membranes containing the functional elements of protein s such as those involved in cell adhesion and signaling.