Brian
S.J. Blagg
Assistant Professor
Medicinal Chemistry
The University of Kansas
Identification of Hsp90 Cochaperones, Immunophilins, and Client Proteins
Mentor:
Robert
P. Hanzlik
The 90kDa heat shock proteins (Hsp90) belong to a family of chaperones that regulate intracellular functions and are required for the refolding of denatured proteins following heat shock as well as the conformational maturations of a large number of key proteins involved in cellular processes. Blagg is exploring a novel proteomics approach toward the identification of Hsp90 client proteins, cochaperones, immunophilins, and multiprotein complexes that fold nascent polypeptides.
The identification of proteins and multiprotein complexes that are bound to Hsp90 will provide insight into the role Hsp90 plays in the maturation of regulatory pathways by the identification of Hsp90 associated proteins and could provide additional targets for cancer chemotherapy. The identification of Hsp90 client proteins will provide evidence for the rational design of future inhibitors that are selective against individual client proteins and help determine the ramifications of inhibition of the entire Hsp90 process.
Using various techniques, Hsp90 dependent proteins from various cancer cell lines will be profiled. Protein profiling of Hsp90 dependent proteins will provide additional insight into the identification of proteins that are under or overexpressed in different cancer cell lines for future applications of Hsp90 inhibition.
Dr. Blagg graduated from the program in 2005 with the award of an R-01 research grant "HTS Assays for Hsp90 Inhibitors." He has since been granted tenure and promoted to associate professor of medicinal chemistry (2007).
Copyright © 2008
Center for Biomedical Research Excellence in Protein Structure and Function
Department of Medicinal Chemistry, School of Pharmacy
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