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W. Andy Tao


  • Professor of Biochemistry
  • Professor of Biochemistry
HANS Room 434

Lab Members

Wiki Lab Page

Google Scholar Page

Area of Expertise: Proteomics and biological mass spectrometry

The mission of our research group is to bridge the gap between technology and biomedical/biochemical 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. Quantitative and functional proteomics in vitro and in living cells using soluble nanopolymers; 2. Phosphorylation imaging and detection; 3. Molecular signaling in cancer cells: phosphoproteomics. 4. Mapping protein-protein and protein-ligand interaction network.

Awards & Honors

(2012) University Faculty Scholar 2011-2014. Purdue University.

(2011) Faculty Scholar. Purdue University.

(2007) Career Award (2007-2012). National Science Foundation.

(2007) Seed for Success. Purdue University.

(2006) Research Award. American Society for Mass Spectrometry.

(2002) Postdoctoral Fellowship. Damon Runyon Cancer Research Foundation.


Tao, W. A. (2009). Materials and methods for isolating phosphopeptides. U.S. Patent No. In pending. Filed on Oct 07, 2009. Washington, D.C.: U.S. Patent and Trademark Office.

Selected Publications

Jayasundera, K. B., Iliuk, A. B., Nguyen, A., Higgins, R., Geahlen, R. L., & Tao, W. A. (2014). Global phosphoproteomics of activated B cells using complementary metal ion functionalized soluble nanopolymers. Anal. Chem., 86, 6363-6371. Retrieved from

Amato, E., Bankemper, T., Kidney, R., Do, T., Onate, A., Thowfeik, F. S., . . . Ma, L. (2014). Investigation of fluorinated and bifunctionalized 3-phenylchroman-4-one (isoflavanone) aromatase inhibitors. Bioorg. Med. Chem., 22, 126-134. Retrieved from

Wang, L., Pan, L., & Tao, W. A. (2014). Specific visualization and identification of phosphoproteome in gels. 86, 6741-6747. Retrieved from

Xue, L., Geahlen, R. L., & Tao, W. A. (2013). Identification of direct tyrosine kinase substrates based on protein kinase assay-linked phosphoproteomics. Mol. Cell Proteomics, 12, 2969-2980.

Xue, L., Wang, P., Wang, L., Renzi, E., Radivojac, P., Tang, H., . . . Tao, W. A. (2013). Quantitative measurement of phosphoproteome response to osmotic stress in arabidopsis based on library-assisted eXtracted Ion chromatogram (LAXIC). Mol. Cell Proteomics, 12, 2354-2369. Retrieved from

Hu, L., Yang, L., Lipchik, A. M., Geahlen, R. L., Parker, L. L., & Tao, W. A. (2013). A quantitative proteomics-based competition binding assay to characterize pITAM-protein interactions. Anal. Chem., 85, 5071-5077. Retrieved from

Iliuk, A. B., & Tao, W. A. (2013). Is phosphoproteomics ready for clinical research?. Clin. Chim. Acta., 420, 23-27. Retrieved from

Xue, L., & Tao, W. A. (2013). Current technologies to identify protein kinase substrates in high throughput. Front. Biol., 8, 216-227. Retrieved from