UCD Physics - RDS

Distinguished Speaker Series 2012

Sickle cell anemia is the first human disease to be understood on a molecular level, beginning with the pioneering 1949 study by the legendary physical chemist, Linus Pauling. The disease is caused by a single base change in DNA that results in an abnormal hemoglobin molecule, the protein in the red cells of blood that delivers oxygen from the lungs to the tissues.  The substitution of a charged amino acid with a neutral one on the surface of the molecule causes the protein to aggregate upon releasing oxygen in the tissues to form helical fibers that stiffen and distort (“sickle”) the red cells and can lead to blockage of small blood vessels. The consequent reduction in oxygen delivery damages many different organs and also results in episodes of very severe pain known as “sickle cell crises.”

Because of its intimate connection to the pathology of sickle cell anemia, this aggregation process has been studied by almost every experimental method of protein physics.  As a result, studies of sickle hemoglobin have become the paradigm for the investigation of other diseases caused by peptide or protein aggregation, such as Alzheimer’s and Parkinson’s diseases.  In this lecture I will describe how a fundamental physical understanding of sickle hemoglobin aggregation has led to a coherent picture of the pathophysiology of the disease as well as new approaches to therapy.

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More information on Dr. William A. Eaton can be found at: http://www.pnas.org/content/106/23/9135.full

For more information contact us at: physics@ucd.ie