Assistant Professor of Chemistry and Chemical Biology
Department of Chemistry and Chemical Biology
12 Oxford Street
Cambridge, MA 02138
Lab Size: Between 5-10
Biological insight to the mechanisms underlying small molecule action in the proteome will require new chemical approaches to access bioactive molecules and precisely evaluate their proteomic activity. The Woo group draws from the fields of chemical biology, organic synthesis, and mass spectrometry to address such areas. Specifically, we develop chemical biology probes to delineate the precise endpoints and functions of a small molecule in the proteome. We concurrently use the power of organic synthesis to access unusual natural product scaffolds and study their biological activity. We then harness the power of liquid chromatography-mass spectrometry (LCMS) to pursue chemical proteomics methods for surveying proteomic interactions of small molecules, natural products, and metabolites like glycans or lipids. In particular, the use of isotope recoding and computational algorithms to detect and identify molecular interactions in the proteome accelerates our mass spectrometry studies. Finally, a bioinformatics and molecular biology approach is taken to reveal the functional relationship between observed molecular interactions and biological phenotype. Studies from the Woo laboratory will have implications in protein targets (and off-targets) for drug discovery, develop synthetic access to novel probes and small molecules, and reveal new mechanisms by which small molecules influence biological systems.
Woo, C. M.; Bertozzi, C. R. “Isotope targeted glycoproteomics (IsoTaG) to characterize intact, metabolically labeled glycopeptides from complex proteomes.” Curr. Protoc. Chem. Bio. 2016, 8, 59.
Woo, C. M.; Li, Z.; Paulson, E.; Herzon, S. B. “Structural basis for DNA cleavage by the potent antiproliferative agent (–)-lomaiviticin A.” Proc. Natl. Acad. Sci. 2016, 11, 2851.
Woo, C. M.; Iavarone, A. T.; Spiciarich, D. R.; Palaniappan, K. K.; Bertozzi, C. R. “Isotope Targeted Glycoproteomics (IsoTaG): A mass independent platform for intact N- and O-glycopeptide discovery.” Nat. Meth., 2015, 12, 561.
Woo, C. M.; Gholap, S. L.; Lu, L.; Kaneko, M.; Li, Z.; Ravikumar, P. C.; Herzon, S. B. “Development of enantioselective synthetic routes to (-)-kinamycin F and (-)-lomaiviticin aglycon.” J. Am. Chem. Soc. 2012, 134, 17262.
Woo, C. M.; Beizer, N. E.; Janso, J. E.; Herzon, S. B. “Isolation of lomaiviticins C-E. Transformation of lomaiviticin C to lomaiviticin A, complete structure elucidation of lomaiviticin A, and structure-activity analyses.” J. Am. Chem. Soc. 2012, 134, 15285.