A Modular Synthesis of Teraryl-based α-Helix Mimetics, Part 5: A Complete Set of Pyridine Boronic Acid Pinacol Esters Featuring Side Chains of Proteinogenic Amino Acids

Melanie Trobe, Till Schreiner, Martin Vareka, Sebastian Grimm, Bernhard Wölfl, Rolf Breinbauer*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

Teraryl-based α-helix mimetics have proven to be useful compounds for the inhibition of protein-protein interactions (PPI). We have developed a modular and flexible approach for the synthesis of teraryl-based α-helix mimetics using pyridine containing boronic acid building blocks to increase the water solubility. Following our initial publication in which we have introduced the methodology in combination with sequential Pd-catalyzed cross-coupling for teraryl assembly, we can now report a complete set of pyridine based boronic acid building blocks decorated with side chains of all proteinogenic amino acids relevant for PPI (Ala, Arg, Asn, Asp, Cys, Gln, Glu, His, Ile, Leu, Lys, Met, Phe, Ser, Thr, Trp, Tyr, Val) to complement the core fragment set. For a representative set of teraryls we have studied the influence of the pyridine rings on the solubility of the assembled oligoarenes.

Original languageEnglish
Article numbere202101280
Number of pages10
JournalEuropean Journal of Organic Chemistry
Volume2022
Issue number17
DOIs
Publication statusPublished - 6 May 2022

Keywords

  • Borylation
  • Cross-coupling
  • Peptide mimetics
  • Protein-protein interactions
  • Pyridine boronic acid pinacol ester

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Organic Chemistry

Fields of Expertise

  • Human- & Biotechnology

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