is in the area of biomolecular self-assembly and biomimetic interfaces.
Our work currently explores the design of peptide molecules that mimic
aspects of natural self-assembly and bio-specific binding. The design
and application of such ‘bottom-up’ assemblies requires precision
synthesis, predictive folding algorithms and accurate characterization
of self-assembly and binding.
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
Folding and Fishing