Introducing our Authors

Protein transmembrane domains are emerging as targets for clinical therapeutics and diagnostic tools. Chemical biologists have studied transmembrane domains in a variety of biological systems, and the fruits of their labors are beginning to surface in the form of rational and high-throughput design methods.

CLC chloride-transport proteins play many critical physiological roles, yet our understanding of these proteins has been limited by a lack of high-affinity inhibitors. This work describes the discovery of novel inhibitors derived from DIDS, a common low-affinity inhibitor of many anion-transport proteins.

Resistance to existing antibiotics and a dearth of novel antibiotics has become a serious threat to public health. My research interest has been focused on understanding a potential antibiotic target, the peptidoglycan glycosyltransferases (PGTs) involved in bacterial cell wall biosynthesis, using biochemical and structural approaches.

For my Ph.D. work, I achieved formal total synthesis of Taxol, a highly complex anticancer drug, by utilizing an automated synthesizer in the Takahashi lab. I was beginning to be interested in how bioactive small molecules interact with target proteins.

Photonic crystal biosensors have recently been developed by incorporating photonic crystal structures into standardized microplates. The sensors have shown high sensitivity in detection of protein–protein, DNA–protein, protein–small molecule, and cellular interactions.

My research is focused on identifying inhibitors of apoptosis inducing factor (AIF). AIF is a cytotoxic DNA-binding protein involved in caspase-dependent and -independent modes of cell death.