Download Proteins Behaving badly - The University of Oklahoma

SCHOOL OF CHEMICAL, BIOLOGICAL &
MATERIALS ENGINEERING
And
UNIVERSITY OF OKLAHOMA BIOENGINEERING
CENTER
The University of Oklahoma
Norman, Oklahoma
2007 – 2008 Seminar Series
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DR. REGINA MURPHY
PROFESSOR
DEPARTMENT OF CHEMICAL AND BIOLOGICAL ENGINEERING
UNIVERSITY OF WISCONSIN, MADISON
MADISON, WISCONSIN
Will present a seminar on
“PROTEINS BEHAVING BADLY:
PROTEIN MISFOLDING AND AGGREGATION
IN NEURODEGENERATIVE DISEASE”
The spontaneous conversion of soluble proteins or protein fragments into insoluble aggregates with
fibrillar morphology and a regular cross-b sheet structure is linked to a number of neurodegenerative
diseases. These aggregates, called amyloid, are believed to be the root cause of disease pathology.
Although it was once believed that the insoluble aggregates were the biologically active species, a
growing body of data suggests that intermediates along the aggregation pathway, rather than the final
product of aggregation, are responsible for the neuronal dysfunction and death observed in these
diseases. Thus, the pathway and kinetics of aggregation of amyloidogenic proteins and peptides become
biologically relevant. In this talk we will present ongoing research in two specific applications. First, we
are examining the aggregation of beta-amyloid peptide, a protein fragment associated with Alzheimer's
disease. We are particularly interested in the mechanism by which the protein transthyretin regulates
beta-amyloid aggregation kinetics, because there is evidence in transgenic mice studies that transthyretin
protects the mice from beta-amyloid toxicity. Second, we are developing methods to examine the role of
expanded polyglutamine domains in aggregation of proteins associated with Huntington's and related
diseases. We have begun a detailed examination of the role of polyglutamine length and position on
protein stability, misfolding, and aggregation. Our hope is that these studies will contribute to
establishing a physicochemical framework for understanding how, when, and why proteins misfold and
aggregate into biological "bad actors", and for developing novel strategies for intervening in protein
misfolding diseases.
THURSDAY, MARCH 13, 2008
COOKIES AND COFFEE -- 2:15 P.M.
SEMINAR -- 2:30 P.M.
SARKEYS ENERGY CENTER, ROOM M-204
THIS IS A REQUIRED SEMINAR FOR CHE 5971