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Reagentless Cleavage of the Peptide Backbone Using Light-Generated Radicals



Barbara J. Jones, Mathew J. Vergne, David M. Bunk, Laurie E. Locascio, M A. Hayes


A key step for protein identification and characterization is cleavage into distinct fragments. All current cleavage methods require the addition of reagents, either proteolytic enzymes or chemical agents, and often a second reagent to discontinue cleavage. We have developed a selective cleavage process for peptides and proteins that employs light-generated radicals produced from titanium dioxide. These short-lived radicals can be produced in confined regions and time scales, making this technique highly tunable. By shining light on titanium dioxide, under a variety of conditions and morphologies, in the presence of peptides and proteins in solution, selective cleavage is consistently observed at proline residues.


cleavage, hydroxyl radical, peptide backbone, titanium dioxide


Jones, B. , Vergne, M. , Bunk, D. , Locascio, L. and Hayes, M. (2021), Reagentless Cleavage of the Peptide Backbone Using Light-Generated Radicals, Science (Accessed April 20, 2024)
Created October 12, 2021