Scott Pegan, Ph.D.
Pharmaceutical and Biomedical Sciences
|Ph.D. Chemistry and Biochemistry||University of California||San Diego||2006|
|M.Sc. Chemistry and Biochemistry||University of California||San Diego||2002|
|B.Sc. Chemistry and Biochemistry||University of California||Santa Barbara||1994|
- Post-doctoral Experience
- 2006 – 2009 Postdoctoral Research Fellow, Advisor: Dr. Andrew Mesecar, Center for Pharmaceutical Biotechnology, University of Illinois, Chicago, IL.
2006 – 2006 Postdoctoral Research Fellow, Advisor: Dr. Senyon Choe, Salk Institute for Biological Studies, La Jolla, CA.
- Honors and Awards
- 2015 Externally selected as 1 of 170 nation-wide nominees for the Defense Science Study Group
2011-2014 Selected by the University of Denver to be its Early Career Reviewer for National Institutes of Health
2006 Kamen Award for outstanding dissertation in biology & chemistry, University of California,San Diego
1999, 2000 American Legion Award for Scholastic Excellence
- Research Interests
- Dr. Pegan's lab is working to gain a greater understanding of the mammalian innate immune response and how it is modulated, as well as develop new therapeutic templates for emerging diseases. His on-going intent is to investigate the anti-viral type I response through the structural and kinetic study of proteases and ligases involved in the immune response signaling pathway. Through this research a better understanding of the role these proteins play in cellular regulation of the innate anti-viral immune response will occur. Currently, the Pegan lab is working with a model system from Crimean-Congo Hemorrhagic Fever virus (CCHFV), which in itself is a dangerous emerging pathogen exhibited by its recent deadly outbreaks in Turkey and India. Furthermore, CCHF has spread across Asia and Africa and is present particularly in the Middle East transmission. Danger to US was highlighted in 2009 by the death of a US Soldier serving in Afghanistan by CCHFV.
Tuberculosis (TB) is one of the most prevalent infections in the world, and a leader among the causes of mortality in developing countries. The World Health Organization estimates one third of the world’s population is infected with latent TB. With a rise in new cases of active TB and emergence of multidrug resistant strains, MDR-TB and XDR-TB, there is a strong need for development of antibiotics targeting novel pharmacological targets within Mycobacterium tuberculosis. One such drug target for TB is M. tuberculosis’ class II fructose 1,6-bisphosphate aldolase (MtFBA), which is required for bacterial survival and is non-existent in humans. Inhibitors have been developed for class II FBAs; however, they lack specificity and drug-like properties, preventing their translation into viable therapeutic leads. Optimization of these compounds has been historically hindered by a lack of MtFBA structural information and viable drug-like leads. Using the latest in Structural biology and drug discovery techniques, Dr. Pegan intends to generate novel chemical compounds that have potent anti–bacterial features for therapeutics targeting TB and other pathogenic bacteria.
- Representative Publications
- Eisenmesser EZ, Capodagli GC, Armstrong G, Holliday MJ, Isern NG, Zhang F, and Pegan SD., Inherent dynamics within the Crimean-Congo Hemorrhagic fever virus protease are localized to the same region as substrate interactions, Protein Sci. (2015) Jan 6. PMID: 25564798
Capodagli GC, Lee SA, Boehm KJ, Brady KM, Pegan SD., Structural and Functional Characterization of Methicillin-Resistant Staphylococcus aureus's Class IIb Fructose 1,6-Bisphosphate Aldolase. Biochemistry. (2014) Dec 9; 53(48):7604-14. Epub 2014 Nov 21. PMID: 25390935
Zhai X, Go MK, O'Donoghue AC, Amyes TL, Pegan SD., Wang Y, Loria JP, Mesecar AD, Richard JP., Enzyme architecture: the effect of replacement and deletion mutations of loop 6 on catalysis by triosephosphate isomerase. Biochemistry. (2014) Jun 3;53(21):3486-501. Epub 2014 May 22. PMID: 24825099
Deaton MK, Spear A, Faaberg KS, Pegan SD., The vOTU domain of highly-pathogenic porcine reproductive and respiratory syndrome virus displays a differential substrate preference, Virology (2014) Apr. vol. 454–455: 247–253. PMC3992837
Capodagli GC, Sedhom WG, Jackson S, Ahrendt KA, Pegan SD., A noncompetitive inhibitor for M. tuberculosis’s class IIa fructose 1,6-bisphosphate aldolase. Biochemistry, (2014) Jan 14; 53(1):202-13., Epub ahead of print on 2013 Dec 24. PMID: 24325645. PMC4167715