Colin Thorpe

Biography

​B.A., 1969, Cambridge University; Ph.D., 1972, University of Kent at Canterbury; Postdoctoral, 1973 – 1978, University of Michigan

Current Research

Our laboratory discovered a new family of enzymes that are facile catalysts of disulfide bond generation in a wide range of proteins over a variety of cellular locales. 

These QSOX enzymes are found widely - from the smallest free-living eukaryotes to humans.  We have studied the role of QSOX in oxidative protein folding using a range of techniques including enzyme kinetics, rapid reaction studies, absorbance and fluorescence spectroscopy, NMR, and mass spectrometry. 

Building on this work, we are now developing methods to evaluate the thiol/disulfide redox state of mammalian cells – both in culture and within biological tissues. 

We are also developing high-resolution imaging approaches to study the construction and properties of disulfide-rich biomaterials.

Representative Publications

Rapid Bioorthogonal Chemistry Turn-on through Enzymatic or Long Wavelength Photocatalytic Activation of Tetrazine Ligation.  Zhang H, Trout WS, Liu S, Andrade GA, Hudson DA, Scinto SL, Dicker KT, Li Y, Lazouski N, Rosenthal J, Thorpe C, Jia X, Fox JM. (2016)  J Am Chem Soc. 138, 5978-83; PubMed PMID: 27078610

Challenges in the Evaluation of Thiol-reactive Inhibitors of Human Protein Disulfide Isomerase.  Foster, C.K. and Thorpe, C. (2017) Free Radic. Biol. Med. 108, 741-749; PubMed PMID: 28465261

Chemistry and Enzymology of Disulfide Cross-linking in Proteins.  Fass, D. and Thorpe, C. (2018) Chemical Reviews 118, 1169-1198;   PubMed PMID: 28699750

Designing Flavoprotein-GFP Fusion Probes for Analyte-Specific Ratiometric Fluorescence Imaging.  Hudson, D.A., Caplan, J.L., and Thorpe, C. (2018)  Biochemistry, 57, 1178-1189;  PubMed PMID: 29341594

Gaussia princeps  luciferase: a bioluminescent substrate for oxidative protein folding.  Yu, T, Laird, J.R., Prescher, J.A., and Thorpe, C.  (2018) Protein Science 27, 1509-1517;  PMID: 29696739