Thioether analogues of the pituitary neuropeptide oxytocin via thiol–ene macrocyclisation of unprotected peptides

Disulfide bonds are an essential feature of many bioactive peptides, however, they are labile to reducing conditions which can limit therapeutic application. Herein, we report an efficient methodology for peptide macrocyclisation, furnishing thioether mimetics of disulfide linkages via thiol–ene cli...

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Bibliographic Details
Published in:Organic & biomolecular chemistry 2022-11, Vol.20 (42), p.8192-8196
Main Authors: Nolan, Mark D., Shine, Conor, Scanlan, Eoin M., Petracca, Rita
Format: Article
Language:English
Subjects:
Chemical synthesis
Disulfide bonds
Oxytocin
Peptides
Pituitary
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Summary:Disulfide bonds are an essential feature of many bioactive peptides, however, they are labile to reducing conditions which can limit therapeutic application. Herein, we report an efficient methodology for peptide macrocyclisation, furnishing thioether mimetics of disulfide linkages via thiol–ene click chemistry. Furthermore, this methodology is applied to the efficient synthesis of analogues of the neuropeptide oxytocin and in a highly efficient route to the clinical therapeutic carbetocin.
ISSN:1477-0520
1477-0539
DOI:10.1039/d2ob01688e