Syntheses of isotopic Rhodamine 6G dyes for relative quantification of proteins by SERRS

ORGN 425

Shirshendu K. Deb, sdeb@purdue.edu1, Dongmao Zhang, zhang17@purdue.edu2, Dor Ben-Amotz, bendor@purdue.edu2, and Vincent J. Davisson, vjd@pharmacy.purdue.edu1. (1) Department of Medicinal Chemistry and Molecular Pharmacology, Purdue University, 1333 Robert Heine Pharmacy Building, West Lafayette, IN 47907, (2) Department of Chemistry, Purdue University, 560 Oval Drive, West Lafayette, IN 47907
Comparative proteomics is essential for the discovery of disease markers, drug targets and disease diagnosis. Realization of these goals depends upon technologies, which allow relative quantification of proteins over a wide range of concentrations. Of late, surface enhanced resonance Raman spectroscopy (SERRS) has been demonstrated as a tool for ultrasensitive detection of biological macromolecules. However, SERRS has not yet been explored as a tool for comparative proteomics. We hypothesized that two isotopic (proteo and deutero) SERRS tags will generate distinct SERRS spectra, thereby enabling relative quantification of proteins from two different samples once they are tagged with two isotopic dyes. Isotopic Rhodamine 6G dyes (a fluorescent dye with ultrahigh SERRS cross-section) were synthesized as shown in the scheme (Scheme 1). We have established that isotopic editing of highly active Rhodamine 6G produces distinct spectral changes. We are currently extending this measurement with proteins covalently labeled with these dyes.

 

Proteins, Peptides, Amino Acids, and Enzymes
1:00 PM-5:00 PM, Tuesday, 15 March 2005 Convention Center -- Room 25A, Oral

Division of Organic Chemistry

The 229th ACS National Meeting, in San Diego, CA, March 13-17, 2005