Proteins are an instructive example from nature of the vast array of structures and functions possible in organic molecules. Most significant to the chemist interested in synthesizing complex functional agents is that proteins accomplish this feat with just 20 amino acid building blocks arranged in sequence-specific polypeptide chains. In our work, we seek to show what is possible to achieve with synthetic macromolecules that are inspired by proteins but expand beyond natural constraints of covalent connectivity.
Through work to date, we have shown how systematic alteration of protein backbone composition, side-chain identity, and chain topology can be used to control folding, impart useful properties, direct self-assembly, provide fundamental insights into biological systems, and create functional mimetics of complex folds. This interdisciplinary research program is situated at the interface of organic chemistry, structural biology, biophysics, and materials science.
Among specific contributions, we have:
Established a design paradigm for the production of artificial backbones with structural complexity rivaling intricate folded architectures found in nature. (leading refs: , ).
Applied protein backbone engineering to probe fundamental issues related to folding, misfolding, and aggregation. (leading refs: , )
Developed methods for creating supramolecular materials with tunable properties through the programmed self-assembly of bio-inspired building blocks. (leading refs: , )
Explored the use of peptides and related bio-inspired scaffolds to modulate electronic and electromechanical properties of inorganic surfaces. (leading ref: )
Invented technologies that stabilize short peptides in specific folded conformations and allow trapping of receptor-bound states of intrinsically disordered ligands in situ. (leading refs: , )
Want to learn more? Browse through our publications.