Closing lecture

Stephen Kent. Ph.D.

Stephen Kent received his undergraduate education in Chemistry and Biochemistry at Victoria University of Wellington, New Zealand, an MSc. in Chemistry and Biochemistry from Massey University, New Zealand, and his Ph.D. in Organic Chemistry at the University of California, Berkeley. Currently, he is Professor of Chemistry at the University of Chicago.

Professor Kent develops advanced synthetic chemistries, and uses them to elucidate the molecular basis of protein function. His early work focused on understanding the underlying physical chemical principles of polymer-supported peptide synthesis, solid phase peptide synthesis, SPPS, and on identifying and eliminating the chemical side reactions then affecting SPPS. The resulting highly optimized methods for the chemical synthesis of peptides were applied to studies of the hepatitis B virus and HIV. With Robert Neurath, this work culminated in elucidation of key information for the development of modern hepatitis B vaccines, and in the use of total chemical synthesis for the determination, with collaborators, of the original crystal structures of the HIV-1 protease protein molecule complexed with canonical inhibitors. These HIV-1 protease structural data formed the basis of the highly successful, worldwide programs in structure based drug design that led to the development of the "protease inhibitor" class of AIDS therapeutics.

In the 1990s, the Kent research group at TSRI pioneered a radically new approach to the total synthesis of proteins, based on "chemical ligation," the chemoselective condensation of unprotected peptide segments in aqueous solution. The chemical ligation principle, embodied in native chemical ligation and kinetically controlled ligation, has enabled the fully convergent total synthesis of protein molecules and the consequent general application of physical and organic chemistry to the world of proteins.

The focus of the Kent laboratory at The University of Chicago is to understand the chemical basis of protein function, and to demonstrate that knowledge by the design and construction of protein molecules with novel structures and properties. In the past few years, the Kent lab has pioneered the use of mirror image protein molecules, D-proteins, to enable the determination of the X-ray structures of recalcitrant proteins by racemic and quasi-racemic crystallography. Even more recently, the Kent lab has reported the first efficient route to a total chemical synthesis of human insulin, making use of a unique ester-linked polypeptide as a chemical-surrogate for proinsulin. Currently, the Kent lab and its collaborators are employing a systematic chemical protein synthesis plus protein phage display approach to develop D-protein molecules as a novel class of molecules for antagonizing the action of natural protein molecules. Such D-protein antagonists may have significant advantages as human therapeutics.

Stephen Kent

Dr. Stephen Kent

Stephen Kent - Honors

Leach Medal, Lorne Conference on Protein Structure & Function, Australia
Bader National Award in Bioorganic Chemistry, American Chemical Society
Akabori Memorial Medal, Japanese Peptide Society
Rudinger Memorial Medal, European Peptide Society
Merrifield Award, American Peptide Society
du Vigneaud Award, American Peptide Society
Kaiser Memorial Award, The Protein Society
Hirschmann National Award in Peptide Chemistry, American Chemical Society
Honorary Fellow, Royal Society of New Zealand
Fellow, Royal Society of Chemistry
Fellow, American Association for the Advancement of Science

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