Journal
CHEMISTRY-A EUROPEAN JOURNAL
Volume 23, Issue 14, Pages 3490-3495Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/chem.201700128
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Funding
- Lundbeck Foundation
- Carlsberg Foundation
- Vietnam International Education Development
- Novo Nordisk Foundation
- Academy of Sciences of the Czech Republic [RVO: 61388963]
- Lundbeck Foundation [R181-2014-3537] Funding Source: researchfish
- Novo Nordisk Fonden [NNF11OC1014446] Funding Source: researchfish
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The introduction of macrocyclic constraints in peptides (peptide stapling) is an important tool within peptide medicinal chemistry for stabilising and pre-organising peptides in a desired conformation. In recent years, the copper-catalysed azide-alkyne cycloaddition (CuAAC) has emerged as a powerful method for peptide stapling. However, to date CuAAC stapling has not provided a simple method for obtaining peptides that are easily diversified further. In the present study, we report a new diversity-oriented peptide stapling ( DOPS) methodology based on CuAAC chemistry. Stapling of peptides incorporating two azidemodified amino acids with 1,3,5-triethynylbenzene efficiently provides (i, i+7)- and ( i, i+9)- stapled peptides with a single free alkyne positioned on the staple, which can be further conjugated or dimerised. A unique feature of the present method is that it provides easy access to radiolabelled stapled peptides by catalytic tritiation of the alkyne positioned on the staple.
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