Catalysis of oxidative protein folding by small-molecule diselenides.

Catalysis of oxidative protein folding by small-molecule diselenides. Research Abstract Details 

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Catalysis of oxidative protein folding by small-molecule diselenides. Abstract Text:

The production of recombinant, disulfide-containing proteins often requires oxidative folding in vitro. Here, we show that diselenides, such as selenoglutathione, catalyze oxidative protein folding by O 2. Substantially lower concentrations of a redox buffer composed of selenoglutathione and the thiol form of glutathione can consequently be used to achieve the same rate and yield of folding as a standard glutathione redox buffer. Further, the low p K a of selenols extends the pH range for folding by selenoglutathione to acidic conditions, where glutathione is inactive. Harnessing the catalytic power of diselenides may thus pave the way for more efficient oxidative protein folding.

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Catalysis of oxidative protein folding by small-molecule diselenides. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Biochemistry

VOLUME: 47

Page Numbers: 6985-7

Journal Abbreviation: Biochemistry

ISSN: 1520-4995

DAY: 14

MONTH: 06

YEAR: 2008

Catalysis of oxidative protein folding by small-molecule diselenides. Information

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LANGUAGE: eng

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Grant and Affiliation Information for Catalysis of oxidative protein folding by small-molecule diselenides.

AFFILIATION: Laboratorium für Organische Chemie, ETH Zürich, Hönggerberg HCI F339, CH-8093 Zürich, Switzerland.

Country: United States

AGENCY: United States NIGMS

GRANT: 1 F32 GM071126-01A1

ACRONYM: GM

MEDLINETA: Biochemistry

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