Peptide cyclisation promoted by supramolecular complex formation.

ABSTRACT: Phenol ester activated dipeptides that are reluctant to ring-close have been cyclised with the aid of sterically shielding metallo-porphyrins avoiding unwanted intermolecular reactions. The binding of ZnTPP to the dipyridine-functionalised activating phenolic ester was studied by NMR titrations and modelling. Staudinger-mediated cyclisations in the presence of ZnTPP increased the yield of the cyclic dipeptide from 16% to 40%.

SUBMITTER: Hartendorp APT 

PROVIDER: S-EPMC8767553 | biostudies-literature | 2022 Jan

REPOSITORIES: biostudies-literature