Two‐Chain Insulin from a Single‐Chain Branched Depsipeptide Precursor: The End of a Long Journey | Zendy

Musiol HansJürgen | Zendy; Moroder Luis | Zendy

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Two‐Chain Insulin from a Single‐Chain Branched Depsipeptide Precursor: The End of a Long Journey

Author(s) -

Musiol HansJürgen,

Moroder Luis

Publication year - 2010

Publication title -

angewandte chemie international edition

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.831

H-Index - 550

eISSN - 1521-3773

pISSN - 1433-7851

DOI - 10.1002/anie.201003018

Subject(s) - depsipeptide , proinsulin , chain (unit) , chemistry , saponification , cystine , folding (dsp implementation) , insulin , stereochemistry , topology (electrical circuits) , combinatorial chemistry , biochemistry , cysteine , biology , physics , mathematics , engineering , combinatorics , astronomy , electrical engineering , enzyme , endocrinology

Coupled chains : A fully synthetic single‐chain branched depsipeptide precursor lacking a proinsulin‐like tethering of the A and B chains leads, by oxidative folding to the insulin characteristic cystine topology and by subsequent saponification of the ester bond, to the target two‐chain insulin molecule with high efficiency (see picture; violet/blue A/B chain, yellow cystine units).

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