This project is the product of collaboration with colleagues Drs. Leslie Poole (Department of Biochemistry) and S. Bruce King (Department of Chemistry) at Wake Forest. Over the past 10-plus years, their groups have developed chemical tools for investigating and quantifying oxidative modifications of protein cysteine thiols focusing onprotein sulfenylation.
Current protein sulfenylation probes display a broad range of reactivity profiles and are compatible with both in vitro cell culture and in vivo studies. Quantitative analysis of labeled sulfenylated proteins can be performed by mass spectrometry, Western blotting and imaging (e.g., application of the BP1 reagent in imaging of tumor samples, Antioxid. Redox Signal., 2014). A new series of protein sulfenylation probes are being targeted to mitochondria to enable studies of global or targeted protein sulfenylation in this key subcellular organelle (e.g., DCP-NEt2C, Sci Reports, 2018). Current work focuses on further development of this chemistry to advance research, diagnosis and treatment of diseases through PET imaging.