Human Cytochrome P45017A1 (CYP17) catalyzes the 17 alpha-hydroxylation of pregnenolone and progesterone as well as the subsequent 17,20 carbon-carbon lyase chemistry of its hydroxylated products. CYP17 function plays a central role in human steroid hormone biosynthesis, and its activity is absolutely essential for the formation of androgens. Thus, inhibition of CYP17 has recently been exploited in the treatment of androgen dependent malignancies. Through application of nanotechnology and biophysical tools, we have identified novel characteristics of CYP17 chemistry that may guide development of the next generation of mechanism-based inhibitors.
After spending his adolescence in the Chicago suburbs, Michael Gregory attended DePauw University where he earned a bachelor's degree in biochemistry in 2008. Following graduation, he returned to the Chicago area and joined the R&D division of a major biopharmaceutical company where he assisted development of protein based therapies for the treatment of pulmonary disorders. In 2009, he came to the University of Illinois and is currently a biochemistry graduate student working in the laboratory of Dr. Stephen Sligar. Here he is studying the steroidogenic enzyme Cytochrome P450c17 (CYP17), which catalyzes the first committed step in androgen formation. As a result of CYP17's role as gatekeeper to androgen biosynthesis it is a front line target in the fight against castration-resistant prostate cancer, which proliferates in response to androgen receptor activation. Michael hopes to integrate knowledge gleaned from rigorous biophysical characterization of CYP17 catalysis with emerging diagnostic and nanotechnologies to encourage development of next-generation therapeutics for the treatment of androgen responsive malignancies such as castration-resistant prostate cancer.
From Michael Gregory's M-CNTC page
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1000 MNTL, University of Illinois, Urbana-Champaign, Urbana, IL