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Jennifer (Jenny) Peeler

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Jennifer (Jenny) Peeler

Assistant Professor of Chemistry

Department/Office Information

Chemistry
104 Wynn Hall

Contact

(315) 228-7245

My educational background and research interests both lie at the intersection of chemistry and biology. Specifically, I focus on exploring biological systems using chemical tools.

In the Peeler Lab, we are studying biological oxidation-reduction (or redox) reactions. We are interested in understanding redox reactions that support cellular function as well as understanding how cells respond to oxidative stress. We specifically focus on redox-active enzymes that possess modified or atypical amino acids. Such enzymes are challenging to produce using traditional molecular biology, but we are able to express these proteins through genetic code expansion. Genetic code expansion allows for the incorporation of non-canonical amino acids into proteins in living cells. This approach allows us to generate homogenous samples of modified or otherwise atypical proteins which can be functionally compared to their unmodified, typical forms. These functional studies inform our understanding of redox biology.

Undergraduate researchers in the Peeler Lab gain experience in several chemical biology and biochemistry techniques, including molecular cloning, tissue culture, protein expression and purification, and enzyme assays.

ºÚÁÏÍø students who are interested in joining the lab are encouraged to contact Professor Peeler.

  • Boston College, NIH postdoctoral fellow (2017 – 2020)
  • The Rockefeller University, PhD in Chemical Biology and Signal Transduction (2017)
  • Franklin & Marshall College, BA in Chemistry and Biochemistry & Molecular Biology (2010)

Biochemistry; Chemical biology; Redox Biology; Genetic code expansion; Selenoproteins; Post-translational modifications

Peeler, J.C. , and Weerapana, E. (2021) Expression of selenoproteins via genetic code expansion in mammalian cells. Methods in Enzymology 662, 143-158.

Peeler, J.C. , Falco, J.A., Kelemen, R.E., Abo, M., Chartier, B.V., Edinger, L.C., Chen, J., Chatterjee, A., and Weerapana, E. (2020) Generation of Recombinant Mammalian Selenoproteins through Genetic Code Expansion with Photocaged Selenocysteine. ACS Chemical Biology 15, 1535-1540.

Italia, J.S., Peeler, J.C. , Hillenbrand, C.M., Latour, C., Weerapana, E., and Chatterjee, A. (2020) Genetically encoded protein sulfation in mammalian cells. Nature Chemical Biology 16, 379-382.

Peeler, J.C. , and Weerapana, E. (2019) Chemical-biology approaches to interrogate the selenoproteome. Accounts of Chemical Research 52, 2832-2840.

Italia, J.S., Addy, P.S., Erickson, S.B., Peeler, J.C. , Weerapana, E., and Chatterjee, A. (2019). Mutually Orthogonal Nonsense-Suppression Systems and Conjugation Chemistries for Precise Protein Labeling at up to Three Distinct Sites. Journal of the American Chemical Society 141, 6204–6212.

Rico, C.A., Berchiche, Y.A., Horioka, M., Peeler, J.C., Lorenzen, E., Tian,H., Kazmi, M.A., Fürstenberg, A., Gaertner, H., Hartley, O., Sakmar, T.P, and Huber, T. (2019). High-Affinity Binding of Chemokine Analogs that Display Ligand Bias at the HIV-1 Co-receptor CCR5. Biophyical Journal 117, 903-919.

Peeler, J.C. , Schedin-Weiss, S., Soula, M., Kazmi, M.A., and Sakmar, T.P (2017). Isopeptide and ester bond ubiquitination both regulate degradation of the human dopamine receptor 4. Journal of Biological Chemistry 292, 21623–21630.

Seitchik, J.L., Peeler, J.C. , Taylor, M.T., Blackman, M.L., Rhoads, T.W., Cooley, R.B., Refakis, C., Fox, J.M., and Mehl, R.A. (2012). Genetically Encoded Tetrazine Amino Acid Directs Rapid Site-Specific in Vivo Bioorthogonal Ligation with trans Cyclooctenes. Journal of the American Chemical Society 134, 2898–2901.

Peeler, J.C ., and Mehl, R.A. (2012). Site-specific incorporation of unnatural amino acids as probes for protein conformational changes. Methods in Molecular Biology 794, 125-134.

Peeler, J.C .*, Woodman, B.F*., Averick, S., Miyake-Stoner, S.J., Stokes, A.L., Hess, K.R., Matyjaszewski, K., and Mehl, R.A. (2010). Genetically Encoded Initiator for Polymer Growth from Proteins. Journal of the American Chemical Society 132, 13575-13577.

*These authors contributed equally to this work.

Stokes, A.L., Miyake-Stoner, S.J., Peeler, J.C., Nguyen, D.P., Hammer, R.P., and Mehl, R.A. (2009). Enhancing the utility of unnatural amino acid synthetases by manipulating broad substrate specificity. Molecular BioSystems 5, 1032–1038.

Miyake-Stoner, S.J., Miller, A.M., Hammill, J.T., Peeler, J.C ., Hess, K.R., Mehl, R.A., and Brewer, S.H. (2009). Probing Protein Folding Using Site-Specifically Encoded Unnatural Amino Acids as FRET Donors with Tryptophan. Biochemistry 48, 5953-5962.

  • CHEM 101: General Chemistry I
  • CHEM 102: General Chemistry II
  • CHEM 353: Proteins and Nucleic Acids
  • CHEM 385: Biophysical Chemistry Methods
  • CHEM 452: Metabolic Chemistry
  • CHEM 454: Bioenergetics
  • CHEM 481/482: Advanced Chemistry Research