Oxidative Modification of Tryptophan-Containing Peptides

Jonas Petersen, Pia Katrine Christensen, Mathias T Nielsen, Kim T. Mortensen, Vitaly V. Komnatnyy, Thomas E. Nielsen, Katrine Qvortrup*

*Corresponding author for this work

Research output: Contribution to journalJournal articleResearchpeer-review

192 Downloads (Pure)

Abstract

We herein present a broadly useful method for the chemoselective modification of a wide range of tryptophan-containing peptides. Exposing a tryptophan-containing peptide to 2,3-dichloro-5,6-dicyano-1,4-benzoquinone (DDQ) resulted in a selective cyclodehydration between the peptide backbone and the indole side chain of tryptophan to form a fully conjugated indolyl-oxazole moiety. The modified peptides show a characteristic and significant emission maximum at 425 nm, thus making the method a useful strategy for fluorescence labeling.
Original languageEnglish
JournalA C S Combinatorial Science
Volume20
Issue number6
Number of pages6
ISSN2156-8952
DOIs
Publication statusPublished - 2018

Keywords

  • Fluorescent labeling
  • Site-selective protein modification
  • Solid-phase peptide synthesis
  • Tryptophan

Cite this

Petersen, J., Christensen, P. K., Nielsen, M. T., Mortensen, K. T., Komnatnyy, V. V., Nielsen, T. E., & Qvortrup, K. (2018). Oxidative Modification of Tryptophan-Containing Peptides. A C S Combinatorial Science, 20(6). https://doi.org/10.1021/acscombsci.8b00014