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Peptide stapling by late-stage Suzuki-Miyaura cross-coupling
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1860-5397-18-1.pdf
Date
2022-01-01
Author
Gruss, Hendrik
Feiner, Rebecca C.
Mseya, Ridhiwan
Schroeder, David C.
Jewginski, Michat
Mueller, Kristian M.
Latajka, Rafat
Marıon, Antoıne
Sewald, Norbert
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Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License
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The development of peptide stapling techniques to stabilise alpha-helical secondary structure motifs of peptides led to the design of modulators of protein-protein interactions, which had been considered undruggable for a long time. We disclose a novel approach towards peptide stapling utilising macrocyclisation by late-stage Suzuki-Miyaura cross-coupling of bromotryptophan-containing peptides of the catenin-binding domain of axin. Optimisation of the linker length in order to find a compromise between both sufficient linker rigidity and flexibility resulted in a peptide with an increased alpha-helicity and enhanced binding affinity to its native binding partner beta-catenin. An increased proteolytic stability against proteinase K has been demonstrated.
Subject Keywords
accelerated molecular dynamics
,
halotryptophan
,
intrinsically disordered peptides
,
late-stage diversification
,
macrocyclisation
,
molecular dynamics
,
stapled peptides
,
Suzuki-Miyaura cross-coupling
,
ACCELERATED MOLECULAR-DYNAMICS
,
ALPHA-HELICAL PEPTIDES
,
ENZYMATIC HALOGENATION
,
TRYPTOPHAN
,
ARYLATION
,
MACROCYCLIZATION
,
DIVERSIFICATION
,
MILD
,
SIMULATIONS
,
STABILITY
URI
https://hdl.handle.net/11511/95357
Journal
BEILSTEIN JOURNAL OF ORGANIC CHEMISTRY
DOI
https://doi.org/10.3762/bjoc.18.1
Collections
Department of Chemistry, Article
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H. Gruss et al., “Peptide stapling by late-stage Suzuki-Miyaura cross-coupling,”
BEILSTEIN JOURNAL OF ORGANIC CHEMISTRY
, vol. 18, pp. 0–0, 2022, Accessed: 00, 2022. [Online]. Available: https://hdl.handle.net/11511/95357.