Regio- and chemoselective covalent immobilization of proteins to gold surfaces through unnatural amino acids

ORGN 456

Rochelle F. H. Bohaty, hawkins@sulphur.chem.utah.edu, Department of Chemistry, University of Utah, 315 S 1400 E, Salt Lake City, UT 84112 and C. Dale Poulter, poulter@chem.utah.edu, Department of Chemisty, University of Utah, 315 South 1400 East, Salt Lake City, UT 84112.
A general strategy for immobilizing soluble proteins regio-and chemoselectively to surfaces through an unnatural amino acid created by post-translational modification of a cysteine residue by Protein Farnesyl Transferase is described. This approach permits one to introduce function groups suitable for bioorthogonal coupling reactions, such as azide and alkyne moieties for “click” and Staudinger reactions, at the carboxy-terminus of natively folded proteins. Here we present our progress towards applying this general immobilization strategy to gold surfaces.
 

New Reactions and Methodology, Total Synthesis, Materials, Devices and Switches, Lipids, Nucleotides and Mimetics
8:00 PM-10:00 PM, Tuesday, March 27, 2007 Hyatt Regency Chicago -- Riverside Center, Poster

Division of Organic Chemistry

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