Projects per year
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 a benzene core unit featuring two halide leaving groups of differentiated reactivity in the Pd-catalyzed cross-coupling used for teraryl assembly. The use of para-bromo iodoarene core fragments resolved the issue of hydrolysis during cross-coupling that was observed when using triflate as a leaving group. We report a complete set of para-bromoiodoarene core fragments 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 and Val). In order to be compatible with general cross-coupling conditions, some of the nucleophilic side chains had to be provided in a protected form to serve as stable building blocks.
Original language | English |
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Article number | e202101279 |
Number of pages | 8 |
Journal | European Journal of Organic Chemistry |
Volume | 2022 |
Issue number | 17 |
Early online date | 2022 |
DOIs | |
Publication status | Published - 6 May 2022 |
Keywords
- Imidazole
- Inhibitors
- Peptide mimetics
- Protein-protein interaction
- Suzuki coupling
ASJC Scopus subject areas
- Physical and Theoretical Chemistry
- Organic Chemistry
Fields of Expertise
- Human- & Biotechnology
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Dive into the research topics of 'Modular Synthesis of Teraryl-based alpha-Helix Mimetics, Part 4: Core Fragments with two Halide Leaving Groups Featuring Side Chains of Proteinogenic Amino Acids'. Together they form a unique fingerprint.Projects
- 1 Finished
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FWF - Oligoarenes - Electrooxidative Synthesis of Bis- and Oligoarenes
1/12/15 → 30/11/19
Project: Research project