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.
Pub Type: Journals
cleavage, hydroxyl radical, peptide backbone, titanium dioxide