Bromotryptophans and their incorporation in cyclic and bicyclic privileged peptides

Júlia García-Pindado, Tom Willemse, Rebecca Goss, Bert U. W. Maes, Ernest Giralt, Steven Ballet, Meritxell Teixidó

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)

Abstract

While revisiting biologically active natural peptides, the importance of the tryptophan residue became clear. In this article, the incorporation of this amino acid, brominated at different positions of the indole ring, into cyclic peptides was successfully achieved. These products demonstrated improved properties in terms of passive diffusion, permeability across membranes, biostability in human serum and cytotoxicity. Moreover, these brominated tryptophans at positions 5, 6, or 7 proved to be compatible as building blocks to prepare bicyclic stapled peptides by performing on-resin Suzuki-Miyaura cross-coupling reactions.
Original languageEnglish
JournalBiopolymers
VolumeEarly View
Early online date12 Mar 2018
DOIs
Publication statusE-pub ahead of print - 12 Mar 2018

Keywords

  • Biostability
  • Bromination
  • On-resin Miyaura and Suzuki-Miyaura cross-coupling
  • PAMPA
  • Solid-phase peptide synthesis
  • Tryptophan

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