Current Research
Protein-protein interactions are involved in several disease pathologies such as autoimmune diseases, cancer, and viral fusion. The clinical success of the antibody Avastin (Genentech) for cancer therapy as well as the a-peptide Fuzeon (Roche) for the inhibition of HIV viral fusion (as well as other antibody therapeutics) have shown that blocking such interactions can benefit patients. Due to the large surface area of these interactions, small molecules usually are not able to target them. However, due to the expense of production and the short half-life, peptide and protein therapeutics have significant disadvantages.
We are working to understand how foldamers, unnatural backbones with defined folding patterns, can be used to block these interactions. Foldamers form helical conformations at short oligomer lengths and are proteolytically stable, making them attractive therapeutically. Based on available structural data (NMR or crystal structures), we try to mimic important contacts with foldamer side chains. Foldamer libraries are then synthesized and tested by a fluorescence polarization assay for binding to the protein of interest, in this case VEGF (Vascular Endothelial Growth Factor). Tight binding foldamers can then be further tested in cell-based assays.
Publications
None at current time
Resume
2009 Resume (word format)
Abstract
2009 Abstract (word format)
Last updated: February 20, 2008