Biophysical Approach to the Structural Characterization of Alpha-Synuclein, A Protein Implicated in Parkinson’s Disease

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Doss-Pepe, Ellen W., Ph.D.
University of Medicine and Dentistry of New Jersey, Robert Wood Johnson
Medical School, Piscataway, New Jersey

Abstract

Alph-synuclein is a protein that has been implicated by data derived from casual studies ob both familiar and sporadic PD. Dr. Ellen Doss-Pepe of R.W. Johnson Medical School (formerly Rutgers) will try to characterize in cell lines the structural and “clumping” properties of this protein, seeking to learn its role in the formation of Lewy Bodies. These inclusionary features are found in brain tissue of PD patients but it is not known whether these deposits (or aggregations) are part of the cause(s) or part of the effects of PD. Neurodegenerative disorders, in general, seem to be linked to the presence of such protein deposits, although the proteins are different in each disease.

Progress Report (as of 8/2002)

Proteins are long chains of amino acids that fold and unfold within cells. The brain has systems of removing and degrading protein constructs when they are no longer in use. Some, however, aggregate and are thought to do damage when they cannot be deleted via these natural systems. Alpha- and beta-synuclein are two such proteins that Dr. Ellen Doss-Pepe (R.W. Johnson Medical School) has worked to characterize in the PD brain, and she has used her PDF funding to create a biochemical assay that distinguishes one from another. Her assay shows that these very similar proteins have important differences in their ways of deposition and clearance in the brain. With these data, she has applied for and been granted follow up funding from the National Institute on Aging (NIH).

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