William A. Eaton is an NIH Distinguished Investigator in NIDDK, Bethesda, Maryland. Dr. Eaton is a biophysical scientist, best known for his physical chemistry investigations of sickle cell hemoglobin polymerization, protein folding, and hemoglobin allostery. His work on sickle cell disease advanced our understanding of molecular pathogenesis and improved treatment; his introduction of photochemical triggering with nanosecond laser pulses, laser temperature jump, and single molecule spectroscopy transformed kinetic studies of protein folding; his single crystal optical absorption and laser photolysis experiments led to an extension of the allosteric model of Monod, Wyman, and Changeux to include tertiary conformations and increase our understanding of how hemoglobin functions. Dr. Eaton was born and educated in Philadelphia, earning a B.A. degree in Chemistry in 1959, an M.D. degree in 1964, and a Ph.D. degree in Molecular Biology in 1967, all at the University of Pennsylvania. In 1968, he moved to the National Institutes of Health (NIH) in Bethesda, Maryland, to fulfill his military service obligation as a Medical Officer in the US Public Health Service. Since 1986 he has served as Chief of the Laboratory of Chemical Physics, the principal laboratory at NIH carrying out research in the biophysical sciences.

Research Interests

Dr. Eaton has almost completely stopped his research on protein folding and hemoglobin allostery to focus on drug treatment for sickle cell disease. There have been tremendous advances recently in curative treatments of sickle cell disease by stem cell transplantation and gene therapy However, such treatments require advanced medical facilities, which are not available to the more than 95% of patients in the world suffering from sickle cell disease who live in under-resourced counties, such as in sub-Saharan Africa or regions of India. The goal of the Eaton lab is to discover an inexpensive oral drug from screening large compound libraries with a high throughput kinetic assay, based on his former discoveries of nucleated sickle hemoglobin polymerization, that is directly relevant to the pathophysiology. (see William A. Eaton and H. Franklin Bunn. "Treating sickle cell disease by targeting HbS polymerization". Blood 129, 2719-2726 (2017). His lab is also collaborating on clinical drug trials with NIH hematologists by monitoring sickling properties of patient's blood

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Primary Section

Section 29: Biophysics and Computational Biology

Secondary Section

Section 14: Chemistry