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David Drewry

Associate Professor

David Drewry, Ph.D.

Associate Professor, Structural Genomics Consortium UNC


(919) 962-5349
120 Mason Farm Road, 1079 GMB, CB# 7356, Chapel Hill, NC, 27599-7356



David Drewry, Ph.D., is a renowned leader in the medicinal chemistry of protein kinases and is one of the principal architects of the research strategy at the SGC-UNC to build an open and collaborative research network to promote target discovery. He previously enjoyed more than 24 years as a medicinal chemist with GlaxoSmithKline and legacy companies, where he led teams working across the preclinical spectrum of drug discovery. His research interests include the art and science of medicinal chemistry, kinase inhibitor design, utilization of annotated sets of kinase inhibitors to build understanding of signaling networks and precompetitive chemical biology to facilitate target identification. After earning a Bachelor’s of Science degree, cum laude, in chemistry from Yale University, Drewry earned his doctorate at the University of California, Berkeley in the laboratory of Paul Bartlett, working on the design, synthesis and mechanistic studies of zinc protease inhibitors. Drewry spent one year as the head of chemistry at Meryx Pharmaceuticals, a biotech startup focused on small-molecule inhibitors of Mer kinase that was a spinoff from the UNC Eshelman School of Pharmacy.


View David Drewry’s Publications

Select Book Chapters

  • Brown, J. R., Drewry, D., Gamo, F.-J. and Garcia-Bustos, J. F. (2013) “Kinase Inhibitors Among Hits from Malaria Cellular Screens”, in Protein Phosphorylation in Parasites Novel Targets for Antiparasitic Intervention (eds C. Doerig, G. Späth and M. Wiese), Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim, Germany. DOI: 10.1002/9783527675401. Chapter 13. ISBN-13: 978-3527332359.

  • Drewry, D.H.; Bamborough, P.; Schneider, K.; Smith, G.K. (2011) “The Kinome and its Impact on Medicinal Chemistry”, in Kinase Drug Discovery (eds R.A. Ward and F. Goldberg), RSC Publishing, DOI:10.1039/9781849733557. Chapter 1. Print ISBN: 978-1-84973-174-4, PDF eISBN: 978-1-84973-355-7.

  • Adams, J.L.; Bamborough, P.; Drewry, D.H.; Shewchuk, L. (2009) “Strategies for Discovering Kinase Drugs”, in Gene Family Targeted Molecular Design (ed K. Lackey). John Wiley & Sons, Inc. Hoboken, NJ, USA, DOI: 10.1002/9780470423936. Chapter 5. ISBN: 978-0-470-41289-3.

  • “Interplay among enzyme mechanism, protein structure, and the design of serine proteases inhibitors”, P. A. Bartlett, N. S. Sampson, S. H. Reich, D. H. Drewry, L. A. Lamden, in Use of X-Ray Crystallography in the Design of Antiviral Agents, Ed: W.G. Laver and G. M. Air, Publisher: Academic Press, Inc., 1990.

Kinase Chemogenomic Set (KCGS)

With the help of partners in academia and industry we are building and sharing the KCGS, a set of kinase inhibitors useful for phenotypic screening to help identify kinase vulnerabilities.

Chemical Probe Projects

Chemical probes (potent, selective, and cell-active compounds) are valuable tools for understanding protein function in disease relevant cellular systems. The list of targets for which we are generating chemical probes changes, but usually includes a range of understudied kinases, such as CAMKK2, STK3, CDK16/17/18, MAP3K19, EPHB6, and members of the NEK family.

Brachyury drug discovery

The transcription factor brachyury is a key driver and vulnerability of the rare cancer chordoma. We are using a structure driven approach to identify small molecule binders that modulate brachyury function in cancer cells. We will use these molecules to understand details of brachyury signaling in cancer cells. Our goal is to demonstrate the druggability of brachyury and help identify a new class of medicine for chordoma patients.

Targeting kinases for malaria

There is still tremendous unmet need in malaria, and resistance to current therapies is a growing problem. We want to leverage our kinase inhibitor experience to help identify new malaria targets and lead molecules for drug discovery. To that end we have a collaborative project in which we are optimizing inhibitors for kinases from plasmodium falciparum.