Timothy Foley, Ph.D., Associate Professor of Chemistry

Understanding how living cells sense and transmit changes in the chemical environment is critical to our comprehension of health and disease.  Proteins, polymers of amino acids that fold into unique shapes with unique chemical properties, are the products of our genetic code.  They perform most of the functions required by living cells and underlie the ability of cells to respond and adapt to changes in the chemical environment.  Much of life at the molecular level involves the partial or complete transfer of electrons in what are known as oxidation-reduction, or redox, reactions.  However, little is known about how cells sense changes in the intracellular redox state.  It is increasingly recognized that unusually reactive sulfur atoms on some proteins may render these proteins especially sensitive to changes in the redox environment of the cell. 

Work in the Foley lab has led to the development of a method to chemically label and, subsequently, capture redox-sensing proteins from crude tissues so that some of these proteins can be identified and the complex structural requisites for highly reactive sulfur atoms can begin to be established.  Using this method, which exploits the affinity of sulfur for arsenic, researchers in the Foley lab have demonstrated that triosephosphate isomerase (TPI), an enzyme involved in glucose metabolism, is among the proteins from the rat brains employed as an experimental model that are most highly sensitive to redox changes.  Work in this lab is underway to learn why the sulfur atoms of TPI are so highly reactive.  It is hoped that the information gathered in these studies can be applied to the prediction and experimental confirmation of redox sensing proteins in humans. 

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