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Issue 43, 2014
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Organocatalysts of oxidative protein folding inspired by protein disulfide isomerase

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Abstract

Organocatalysts derived from diethylenetriamine effect the rapid isomerization of non-native protein disulfide bonds to native ones. These catalysts contain a pendant hydrophobic moiety to encourage interaction with the non-native state, and two thiol groups with low pKa values that form a disulfide bond with a high E°′ value.

Graphical abstract: Organocatalysts of oxidative protein folding inspired by protein disulfide isomerase

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Article information


Submitted
14 Aug 2014
Accepted
17 Sep 2014
First published
18 Sep 2014

Org. Biomol. Chem., 2014,12, 8598-8602
Article type
Communication
Author version available

Organocatalysts of oxidative protein folding inspired by protein disulfide isomerase

J. C. Lukesh III, K. A. Andersen, K. K. Wallin and R. T. Raines, Org. Biomol. Chem., 2014, 12, 8598
DOI: 10.1039/C4OB01738B

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