Abstract
The in vitro oxidative folding of disulfide-rich proteins can be challenging. Here we show a new class of small molecule diselenides, which can be easily prepared from inexpensive starting materials, used to enhance oxidative protein folding. These compounds were tested on a model protein, bovine pancreatic trypsin inhibitor. Two of the tested diselenides showed considerable improvement over glutathione and were on par with the previously described selenoglutathione.
Original language | English |
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Pages (from-to) | 3336-3339 |
Number of pages | 4 |
Journal | Chemical Communications |
Volume | 52 |
Issue number | 16 |
DOIs | |
State | Published - 2016 |
Bibliographical note
Publisher Copyright:© The Royal Society of Chemistry 2016.