Isolation of specific proteins via copper(I)-catalyzed alkyne-azide “click” cycloaddition

CHED 601

Benjamin C. Buer, buer0033@morris.umn.edu1, Roman V. Rozhkov2, Giselle M. Knudsen3, and V. Jo Davisson3. (1) Department of Chemistry, University of Minnesota-Morris, 600 E 4th St, Morris, MN 56267, (2) Bindley Bioscience Center, Birck Nanotechnology Center and Department of Medicinal Chemistry and Molecular Pharmacology, Purdue University, West Lafayette, IN 47906, (3) Department of Medicinal Chemistry and Molecular Pharmacology, Purdue University, West Lafayette, IN 47906
The isolation of specific proteins from live cells is key to discovering protein complexes involved in protein-drug interactions. Due to its reactivity under biological conditions and orthogonality to functional groups of biomolecules, copper(I)-catalyzed alkyne-azide “click” cycloaddition provides an ideal method for the immobilization of a protein-drug complex to a solid support. Geldanamycin (GA) is an inhibitor of Hsp90, a protein chaperone that is over-expressed in cancer cells, providing a very promising target for anti-cancer drugs. The binding of Hsp90 to GA not only provides a model system for the elucidation of specific proteins with the use of “click” chemistry, but may also reveal unknown Hsp90 binding partners.
 

Undergraduate Research Poster Session: Organic Chemistry
11:00 AM-1:00 PM, Monday, March 26, 2007 Hyatt Regency Chicago -- Riverside Center, Poster

Division of Chemical Education

The 233rd ACS National Meeting, Chicago, IL, March 25-29, 2007