Abstract: Determination of protein cysteine reactivity with fluorescently-labeled glutathione derivatives

This summer I will conduct research with Dr. Lisa Landino’s laboratory team into the potential damage of electron removal from molecules composing a key protein in cellular microtubules by reactive molecular radicals. This electron removal, also called “oxidation,” causes the protein’s subunits to unnaturally bind together, impeding the normal function of microtubules in cells. Since microtubules provide structural support in all cells and are especially important in nerve cells, their impairment may contribute to the development of neurodegenerative diseases such as Alzheimer’s and Parkinson’s. With this in mind, our lab team attempts to study the mechanisms behind neurodegeneration by radical molecules and determine whether or not this protein is involved in hopes of ultimately developing a means of reversing nerve cell damage.

To study these oxidative processes, our laboratory uses glutathione, a protein serving as a first line of defense against radical oxidation. By tracking levels of oxidized and unoxidized (or “reduced”) glutathione in cells, we can identify those cells with potential oxidative damage. We are currently trying to visualize glutathione using fluorescent labels that still allow it to undergo its proper cellular reactions, so this summer I hope to test fluorescently-labeled glutathione’s reactivity with other proteins while changing reaction variables like fluorescent marker type and concentration, pH, temperature, and time. This data will be compiled with other data collected over the summer to create a table comparing the reactivities of glutathione and the rest of our routinely-used proteins labeled with our different fluorescent probes.