A broadband LC-MS technique for simultaneous qualitative and quantitative protein profiling

ANYL 347

Jeffrey C. Silva, jcruzsilva@aol.com1, Scott J. Geromanos, scott_geromanos@waters.com2, Craig A. Dorschel, craig_dorschel@waters.com2, Johannes P. C. Vissers, Hans_Vissers@waters.com2, Minerva A. Hughes, covebay@hotmail.com3, and Craig A. Townsend, ctownsend@jhu.edu3. (1) Protein Chemistry, Cell Signaling Technology, 3 Trask Lane, Danvers, MA 01923, (2) Proteomics Core Technology, Waters Corporation, 34 Maple Street, Milford, MA 01757-3696, (3) Department of Chemistry, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218
Profiling of expressed microbial proteins has diverse applications ranging from the response of bacteria to environmental stimuli as well as pharmaceuticals and disinfectants. Separation methods have been integrated with mass spectrometry to reduce the complexity of biological protein mixtures for efficient monitoring of differential protein expression, but these methods can be time consuming, laborious and not amenable to quantitation. A robust protein profiling method should provide accurate, rapid and reproducible detection of changes in the level of protein expression or presence of new proteins. The intent of this work is to demonstrate a novel LC-MS method for reproducibly monitoring protein expression profiles in model biological systems such as E. coli grown on different carbon sources and probing isoniazid drug response in M. bovis. Principal Component Analysis (PCA) and unattended hierarchical clustering have been performed to demonstrate the analytical reproducibility of the technique and the biological variation among the model systems.
 

Analytical Technology for Drug Discovery
8:30 AM-11:50 AM, Tuesday, August 21, 2007 BCEC -- 105, Oral

Division of Analytical Chemistry

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