We combine chemical biology, enzyme kinetics, proteomics, metabolomics, epigenetics and computational methods to investigate redox-regulated processes with significance to normal physiology and pathology.

Individual research projects fall under three major areas of interest:

  1. Development of Chemical Probes and Methods for Identification of Oxidative Modifications of Protein Thiols
  2. Structure-Function Analysis of Redox Regulated Proteins
  3. Head and Neck Cancer - Prevention, Treatment and Quality of Life.

Redox reactions and associated reactive oxygen and nitrogen species (ROS/RNS) are key drivers of growth and survival in biological systems, and widely acknowledged today as integral regulatory components in signaling, metabolism, and epigenetics.

While the controlled and localized production of ROS/RNS is critical to normal physiology and health, the alteration of redox homeostasis through acute or chronic accumulation of these reactive oxidants leads to numerous pathologies in humans including cancer, cardiovascular diseases, diabetes, and others.

Our Goal

The overarching goal of the research performed in our laboratory is the investigation of the molecular mechanisms linking redox balance to disease development and treatment. Specifically, our research focuses on:

  • Development of Chemical Approaches for the Quantitative Analysis of Protein Thiol Oxidative Modifications
  • The Implications of Akt2 Redox-regulation in Radiation-associated Diabetes and Muscle Function in Aging
  • Head and Neck Cancer Prevention, Treatment and Improvement of Quality of Life

Chemical and analytical methods developed in the context of these projects are further applied to a number of collaborative studies investigating redox effects in aging and osteoarthritis (with Dr. Richard Loeser, University of North Carolina - Chapel Hill), chronic kidney disease (with Dr. Snezana Petrovic), inflammation and sepsis (with Dr. Charles McCall) and few others.

Additionally, our group provides expertise in analysis of enzymes mechanisms and kinetics using mass spectrometry. An example of these studies is the long-standing and productive collaboration with our colleague Dr. Todd Lowther, with whom we investigate the kinetics of peroxiredoxins hyperoxidation and the repair of hyperoxidized protein by sulfiredoxin.

We invite you to explore our lab’s research.