TY  - JOUR
AB  - The development of peptide stapling techniques to stabilise α-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 α-helicity and enhanced binding affinity to its native binding partner β-catenin. An increased proteolytic stability against proteinase K has been demonstrated.
DA  - 2022
DO  - 10.3762/bjoc.18.1
LA  - eng
M2  - 1
PY  - 2022
SP  - 1-12
T2  - Beilstein Journal of Organic Chemistry
TI  - Peptide stapling by late-stage Suzuki–Miyaura cross-coupling
UR  - https://nbn-resolving.org/urn:nbn:de:0070-pub-29603297
Y2  - 2024-11-21T23:13:16
ER  -