![Daniel Murdock](https://stars.library.ucf.edu/ramp_gallery/1065/thumbnail.jpg)
Student
Daniel Murdock
Files
Cohort
2017-2018
Biography
Daniel Murdock was born and raised in Central Florida and has had a lifelong interest in the sciences. He is currently expressing, purifying, and characterizing key metabolic enzymes in Clostridium difficile as an undergraduate researcher in Dr. William Self's lab. He plans to pursue an MD degree and become a physician.
Faculty Mentor
Dr. William T. Self, Associate Director of Undergraduate Affairs & Associate Professor
Undergraduate Major
Biomedical Sciences
Future Plans
MD degree
Profile Links
Disciplines
Medicine and Health Sciences
Recommended Citation
Murdock, Daniel, "Daniel Murdock" (2018). UCF Research and Mentoring Program Scholars. 67.
https://stars.library.ucf.edu/ramp_gallery/67
![Daniel Murdock](https://stars.library.ucf.edu/ramp_gallery/1065/thumbnail.jpg)
Research
Title: Expression, Purification, and Characterization of Clostridium Difficile Thioredoxin Reductase
PI: Dr. Self
Institution: University of Central Florida
Abstract: Clostridium difficile is a hospital-acquired pathogen responsible for a diarrheal condition that kills nearly 30,000 people in the United States annually. The use of broad-spectrum antibiotics disrupts the natural colonic bacterial flora, allowing C. difficile to grow and release toxins. Antibiotic resistance in some C. difficile strains has increased the importance of seeking out novel drug targets. One potential target is thioredoxin reductase (TrxR), an enzyme that allows C. difficile to utilize amino acids as a sole source of carbon and nitrogen. This occurs by Stickland fermentation reactions, which use amino acids as both electron donors and acceptors to harness energy for growth. We hypothesize that a recently identified natural product may be a potential inhibitor of TrxR. In order to test the impact of this natural product on TrxR function, the TrxR gene has been cloned, His-tagged, ligated into an expression vector, and expressed in Escherichia coli. Recombinant TrxR will be purified using affinity and size exclusion chromatography. TrxR accepts electrons from Stickland donors via NADPH, and this process will be characterized from a basic research perspective by measuring the spectral change of 5,5'-Dithiobis(2-nitrobenzoic acid) upon reduction at 412 nm in the presence of NADPH. The effects of the natural product on the activity of C. difficile TrxR will then be measured to determine if it holds therapeutic potential as a treatment for C. difficile infections.