Jeffery W. Kelly was born in New York, USA in 1960. He received his B.S. in chemistry from SUNY Fredonia (1982), his Ph.D. in organic chemistry from the University of North Carolina (1986), and post-doctoral training at The Rockefeller University (1986-89). Currently, he is the Lita Annenberg Hazen Professor of Chemistry at The Scripps Research Institute. Previously, he served as Dean of the Graduate Program, Vice President of Academic Affairs, and Chairman of Molecular Medicine.

An author of > 390 papers (Web of Science h-index = 105), Professor Kelly is an elected member of the National Academy of Sciences, American Academy of Arts and Sciences, the National Academy of Inventors, and the American Chemical Society Medicinal Chemistry Division Hall of Fame. His contributions have been recognized by awards including the Wolf Prize in Chemistry, the Breakthrough Prize in Life Sciences, the Royal Society Robert Robinson Award in Synthetic Organic Chemistry, the American Chemical Society Edward E. Smissman Award, the E.B. Hershberg Award for Important Discoveries in Medicinally Active Substances, the American Institutes of Chemists Chemical Pioneer Award, the Jacob and Louise Gabbay Award in Biotechnology and Medicine, and the Royal Society of Chemistry Jeremy Knowles Award. Kelly has placed 44 trainees in academia and over 70 trainees in the biotechnology and pharmaceutical industries.

Research Interests

The central theme of Kelly lab research is to understand the chemistry and biology influencing the competition between protein folding, misfolding, and aggregation—the latter processes being associated with a spectrum of human diseases. Knowledge gained from these investigations is used to conceive of new therapeutic strategies for diseases of protein conformation.

Kelly and his lab discovered the blockbuster drug tafamidis/Vyndaqel (marketed by Pfizer), the first drug that slows the progression of a human amyloid disease by inhibiting protein aggregation. To do this, he translated a genetic observation into a mechanistic understanding of amyloid disease prevention mediated by slowing misfolding required for aggregation. Tafamidis inhibits transthyretin aggregation by kinetic stabilization of the native transthyretin conformation–it slows the rate-limiting step in aggregation. Tafamidis was the first drug to demonstrate the importance of protein aggregation as a driver of amyloid disease etiology.

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Primary Section

Section 14: Chemistry

Secondary Section

Section 29: Biophysics and Computational Biology