Our research centers around mass spectrometry-based omics measurements for investigating small molecule-proteome reactions and interactions. We develop and use innovative measurement technologies to discover novel reactive sites of protein for mechanistic investigation and chemical manipulation. We are particularly interested in how human aryl hydrocarbon receptor (AhR) and Toll-like receptors (TLRs) interact with molecules in the microbiota and the environment.

MS and proteomics methods for chemically-modified proteins and peptides

  • Chemical principles and measurements of endogenous and exogenous omic reactions
    • Quantitative analysis of proteome-wide reactions with chemicals and metabolites
  • Novel chemical reagents for MS-based proteomics measurements
    • Design and synthesis of reagents enabling new MS analysis with improved sample throughput and signal enhancement
    • Novel chemical probes and proteomics methods for analyzing chemical modifications of proteins in the proteome
    • Fragment-ion based analysis for MS of modified proteins and peptides
  • MS of the in-cell structure of proteins
    • Reversed fast photochemical oxidation of proteins (FPOP)-multiple reaction monitoring (MRM) MS
    • Expression, trafficking, structure, and function of cystic fibrosis transmembrane conductance regulator

Discovery and development of active metabolites and molecular markers

  • Bioactivity-driven (targeted) discovery of molecules in the metabolome
  • New methods of separation and MS for analyzing lipids and metabolites
  • Ultrathroughput MS for biomarker research and applications