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 leaving groups of differentiated reactivity in the Pd-catalyzed cross-coupling used for teraryl assembly. In previous publications we have introduced the methodology of 4-iodophenyltriflates decorated with the side chains of some of the proteinogenic amino acids. We herein report the core fragments corresponding to the previously missing amino acids Arg, Asn, Asp, Met, Trp and Tyr. Therefore, our set now encompasses all relevant amino acid analogues with the exception of His. In order to be compatible with the triflate moiety, some of the nucleophilic side chains had to be provided in a protected form to serve as stable building blocks. Additionally, cross-coupling procedures for the assembly of teraryls were investigated.
Original language | English |
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Article number | e202101278 |
Number of pages | 7 |
Journal | European Journal of Organic Chemistry |
Volume | 2022 |
Issue number | 17 |
Early online date | 2022 |
DOIs | |
Publication status | Published - 6 May 2022 |
Keywords
- Inhibitors
- Peptide mimetics
- Protein–protein interactions
- Suzuki coupling
- Triflate
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 'A Modular Synthesis of Teraryl-Based α-Helix Mimetics, Part 3: Iodophenyltriflate Core Fragments 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