Surfactant-like peptide architectures, “surf-tides”, are capable of self-assembly at the interface between two phases. These peptide-interfaces are constructed such that intramolecular forces control the formation of short-range ordering (< nm), while intermolecular forces promote the formation of long-range crystal structures (um). The particular sequence results in templated assemblies with unique materials characteristics due to the long-range interactions, specific biological binding characteristics, and local chemical functionalization of the individual peptides. This methodology is proving to be an effective tool for engineering drug delivery vehicles, biosensing, and molecular medicines.

We have two ongoing areas of research. First, we use the dynamics inherent in the folding and unfolding of peptides to yield tunable surface activity. Peptides are designed where the folded state is amphiphilic, but the unfolded state is not amphiphilic, resulting in new dynamic peptide architectures that can assemble as a consequence of folding behavior. Second, we examine the phase behavior of peptide monolayers assembled at the air-water interface. Simple amphiphilic peptides show exceptionally complex supramolecular geometries as a function of surface pressure. In both research areas, we seek to understand the fundamental thermodynamics and kinetics of surface active peptides to engineer new biologically inspired materials.