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Late-Stage Modification of Halotryptophan-Containing Peptides Via Negishi Cross-Coupling.

Laura Cerveson1, Marcel-Jannik Heldt1, Norbert Sewald1

  • 1Department of Chemistry, Organic and Bioorganic Chemistry, Bielefeld University, Bielefeld, Germany.

Chemistry (Weinheim an Der Bergstrasse, Germany)
|May 25, 2026
PubMed
Summary

Negishi cross-coupling enables late-stage functionalization of complex bromotryptophan peptides. Optimized conditions and DMSO solvent systems enhance solubility and reactivity for diverse peptide modifications.

Keywords:
amino acidsbromotryptophanlate‐stage modificationmedicinal chemistrynegishi cross‐couplingnon‐proteinogenic amino acidspalladium‐catalyzed coupling reactionspeptidesolubility

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Area of Science:

  • Organic Chemistry
  • Medicinal Chemistry
  • Peptide Chemistry

Background:

  • Late-stage functionalization is crucial for peptide diversification.
  • Negishi cross-coupling offers mild conditions for alkyl group installation.
  • Adapting Negishi coupling for complex peptide substrates remains challenging.

Purpose of the Study:

  • To investigate the applicability of Negishi cross-coupling to bromotryptophan-containing peptides.
  • To optimize reaction conditions for efficient peptide functionalization.
  • To address challenges related to peptide solubility and functional group tolerance.

Main Methods:

  • Systematic optimization of Negishi cross-coupling conditions.
  • Exploration of DMSO and DMSO/DMF solvent systems.
  • Application to model tripeptides and complex pentapeptides with various residues.

Main Results:

  • Optimized protocol achieved efficient cross-coupling of a model tripeptide.
  • DMSO-based solvent systems improved solubility and reactivity for 6- and 7-bromo-l-tryptophan peptides.
  • Demonstrated functional group tolerance for unprotected residues like aspartic acid and serine.
  • Solvent-dependent reactivity observed in pentapeptides, with DMSO systems outperforming DMF.

Conclusions:

  • Negishi cross-coupling is a viable method for late-stage functionalization of bromotryptophan peptides.
  • DMSO-containing solvents are key to overcoming solubility limitations.
  • The developed method allows for diverse modifications of complex peptide structures.