U.S. Department of Health and Human Services
William Eaton
 

 Contact Info

 
Tel: +1 301 496 6030
Email: eaton@helix.nih.gov
 

 Training and Experience

 
Ph.D., University of Pennsylvania, 1967

M.D., University of Pennsylvania, 1964

Free University of Berlin, 1960

B.A., University of Pennsylvania, 1959
 

 Related Links

 

    William A. Eaton, M.D., Ph.D.

    Chief, Laboratory of Chemical Physics
    NIH Distinguished Investigator, Laboratory of Chemical PhysicsBiophysical Chemistry Section
    Specialties: Biomedical Engineering/Biophysics/Physics

    Research Summary

    Research Goal

    The purpose of our research is to understand the physics of protein folding and to discover a drug for sickle cell disease.

    Current Research

    Our current research is both basic and applied. Our basic research is concerned with fundamental aspects of the mechanism of protein folding. A series of novel techniques have been developed to study the dynamics of fast processes in protein folding. These include the use of nanosecond pulsed lasers to trigger and monitor the folding reaction, as well as single molecule fluorescence measurements. Simple theoretical models are used to interpret the experimental results and expose the basic underlying physics of these processes. The experimental results and theoretical modeling are providing critical benchmarks for the construction of a detailed picture of the sequence of events as a protein forms its native conformation from the random structures of the unfolded polypeptide chain.  

    A highly sensitive and pathophysiologically-relevant kinetic assay has been developed to screen compounds for ant-sickling activity. The assay uses laser photolysis to induce sickling and automated image analysis to detect the formation of sickle fibers in individual red cells. As a strategy for the most rapid path to bringing a drug to market, the first phase of the screen is to test all U.S. Food and Drug Administration-approved drugs. 

    Applying Our Research

    Understanding the physics of protein folding is essential for understanding protein mis-folding, the cause of many human diseases, including Alzheimer's disease, type II diabetes, and Parkinson's disease.

    Hydroxyurea is the only drug that is currently used to treat sickle cell disease, and helps, but does not cure, only about 50 percent of patients. Additional drugs are critically needed.

    Need for Further Study

    Further studies should look at making the connections among protein and mis-folding folding theory, experiments, and computer simulations. They should also look at the development of additional drugs for sickle cell disease.