Nature utilizes a "sequence and folding" approach to rapidly construct diverse sets of functional molecules with defined conformations (i.e., RNA and proteins) from a limited set of building blocks. These polymers adopt distinct stable conformations, where the function of the biopolymer is dependent on the sequence, as well as, its three-dimensional structure. An overarching research goal in our lab is to imitate this approach for the production of biomimetic oligomers with well-defined three-dimensional shapes. We are utilizing this strategy in the design and synthesis of organic molecules that allow control over specific protein-protein, protein-nucleic acid, and protein-carbohydrate interactions. To date, our lab has described three synthetic scaffolds:

Hydrogen Bond Surrogate Helices (image right) are stabilized alpha-helices in which one main chain i to i+4 hydrogen bond has been replaced with a carbon-carbon bond. These helices have been shown to target their protein receptors with high affinity.


Oligooxopiperazines (image left) are a new class of nonpeptidic helix mimetics derived from amino acids and featuring chiral backbones. Oligooxopiperazine dimers adopt stable conformations that reproduce the arrangement of i, i+4, and i+7 residues on an alpha-helix.








Triazolamers (image below) are nonpeptidic oligomers in which the peptide bond is replaced with 1,2,3-triazole rings but the chiral main-chain and amino acid side chains are preserved.