Professor Sharp is a world renowned and internationally recognized expert in HRPF. He has published more than 25 peer-reviewed articles in the field of HRPF method development, fundamentals, and applications between 2002 and today, with over forty-five publications overall. Professor Sharp published the first benchtop methods for HRPF, including the first method using UV photolysis of hydrogen peroxide for hydroxyl radical generation. With numerous invited lectures to both academia and private industry on the application of HRPF to biotherapeutics, Dr. Sharp has addressed problems associated with formulation, biosimilarity, aggregation, and protein-protein and protein-ligand interaction mapping. Professor Sharp’s lab is also known for their work in glycosaminoglycan structure-function analysis, and his team commonly leverages their expertise in both areas to study protein-carbohydrate complexes.
Professor Sharp received his PhD in 2003 from a joint program between Oak Ridge National Laboratory and the University of Tennessee, under the mentorship of Dr. Robert Hettich. He performed his postdoctoral studies at the National Institute of Environmental Health Sciences in the Laboratory of Structural Biology, under the supervision of Dr. Kenneth Tomer. In 2007, he joined the University of Georgia’s Complex Carbohydrate Research Center as a research faculty member. Most recently, Professor Sharp joined the faculty at the University of Mississippi School of Pharmacy, where he currently serves as an Associate Professor of Pharmacology and Research Professor of the Research Institute of Pharmaceutical Sciences. He has received multiple awards for excellence in research, most recently winning the New Investigator Research Award from the University of Mississippi School of Pharmacy and being designated the University of Mississippi nominee for the 2019 Blavatnik Award in Life Sciences. Professor Sharp serves on multiple national and international advisory and review panels as an expert on protein and carbohydrate biophysical and structural analysis by mass spectrometry.