Weiguo Andy Tao, Ph.D. Assistant Professor (MCMP Courtesy Appointment) Phone: (765) 494-9605 E-mail: watao@purdue.edu Personal webpage: http://www.biochem.purdue.edu/faculty/tao/index.html Full directory listing

Specialization: Proteomics and biological mass spectrometry

Education

Research: Proteomics and biological mass spectrometry

The mission of our research group is to bridge technology with biomedical discovery. Mass spectrometry-based proteomics is the kind of research that is highly interdisciplinary, bringing together biology, chemistry, instrumentation, statistics, and bioinformatics. Proteomics thus holds significant promise for the discovery of diagnostic or prognostic protein markers, for the detection of new therapeutic targets and as a powerful tool to further our understanding of basic biological processes and mechanisms. The realization of these expectations relies on the development of novel chemistry and instrumentation.

Our group focuses on the development of novel strategies and reagents to efficiently target and discover proteins of important biological relevance as potential biomarkers. Such proteins of interest are typically low in abundance, dynamically expressed, and post-translationally modified. The subject, called targeted proteomics, therefore involves the integration of a number of technologies including the selective targeting of proteins with activities of interest, multi-step sample preparation, and mass spectrometry. Examining changes in these proteins within cells under different physiological conditions will offer insights into understanding cellular and molecular mechanisms that cannot currently be obtained through traditional biological studies that usually focus on the detailed analysis of individual biomolecules.

Current projects in my group are:

1. Functional proteomics in vitro and in living cells using soluble nanopolymers
2. Biomarker discovery using Ossabaw swine as the animal model for metabolic syndrome and cardiovascular disease
3. Profiling of protease substrates in apoptotic cells
4. Molecular signaling in cancer cells: phosphoproteomics

Representative Publications

Galan JA, Guo M, Sanchez EE, Cantu E., Rodriguez-Acosta A, Perez JC and Tao WA. 2008. Quantitative analysis of snake venoms using soluble polymer-based isotope labeling. Mol Cell Proteomics 7(4):785-799.

Tao WA. 2007. Soluble polymers-based isotopic labeling (SoPIL): a new strategy to discover protein biomarkers? Expert Review of Proteomics 4(5):603-607.

Timmer J C, Enoksson M, Wildfang E, Zhu W, Igarashi Y, Denault JB, Ma Y, Dummitt B, Chang YH, Mast AE, Eroshkin A, Smith JW, Tao WA and Salvesen G S. 2007. Profiling constitutive proteolytic events in vivo. Biochem J 407(1):41-48.

Enoksson M, Li J, Ivancic M M, Timmer J, Wildfang E, Eroshkin A, Salvesen G S and Tao WA 2007. Identification of proteolytic cleavage sites by quantitative proteomics. J Proteome Res 6(7):2850-8.

Song Y, Talaty N, Tao WA, Pan Z, Cooks RG. 2007. Rapid ambient mass spectrometric profiling of intact, unteated bacteria desorption electrospray ionization. Chem Commun 61-63.

Guo M, Galan J and Tao WA. 2007. Soluble nanopolymer-based phosphoproteomics for studying protein phosphatase. Methods 42(3):289-297.

Bodenmiller B, Mueller LN, Pedrioli PGA, Pflieger D, Jünger MA, Eng JK, Aebersold R, and Tao WA. 2007. An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: Application to Drosophila melanogaster Kc167 Cells. Mol Biosys 3:275-286.

He XC, Yin T, Grindley JC, Tian Q, Sato T, Tao WA, Dirisina R, Porter-Westpfahl KS, Hembree M, Johnson T, Wiedemann LM, Barrett TA, Hood L, Wu H, Li L. 2007. PTEN-deficient intestinal stem cells initiate intestinal polyposis. Nature Genetics 39(2): 189-198.

Guo M, Galan J, Tao WA. 2007. A novel quantitative proteomics reagent based on soluble nanopolymers. Chem Commun 1251-1253, DOI:10.1039/ B614926J.

Zhou F, Galan J, Geahlen RL, Tao WA. 2007. A Novel quantitative proteomics strategy to study phosphorylation-dependent peptide-protein interactions. J Proteome Res. 6:133-40.