Spectroscopic evidence of the formation of "Goldfingers"

INOR 759

Matthew A. Franzman, franzman@usc.edu, Department of Chemistry, University of Southern California, 840 Downey Way, LJS 256, Los Angeles, CA 90089 and Amy M. Barrios, Deparment of Medicinal Chemistry, University of Southern California, 30 South 2000 East, Salt Lake City, UT 84112.
Although many patients with severe rheumatoid arthritis are treated with Au(I) drugs including auranofin and aurothiomalate, the therapeutic mechanism of these drugs remains a mystery. Gold is likely to interact with many different biological targets including cysteine-dependent enzymes, copper trafficking proteins and metal-responsive transcription factors. The cysteine-rich structural motifs of zinc finger transcription factors are especially attractive targets of Au(I). If Au(I) is able to replace Zn(II), the resultant ‘Goldfinger' protein would have significantly different secondary structures than the parent zinc finger transcription factor, potentially interfering with the production of inflammatory cytokines. In this work, we present spectroscopic evidence for the formation of 'Goldfingers' with an eye toward characterizing one possible pathway for the antiarthritic activity of Au(I).
 

Bioinorganic Chemistry: Enzymes and Coenzymes
7:00 PM-10:00 PM, Tuesday, August 21, 2007 BCEC -- Exhibit Hall - B2, Poster

Sci-Mix
8:00 PM-10:00 PM, Monday, August 20, 2007 BCEC -- Exhibit Hall - B2, Sci-Mix

Division of Inorganic Chemistry

The 234th ACS National Meeting, Boston, MA, August 19-23, 2007