A cysteine selenosulfide redox switch for protein chemical synthesis

Vincent Diemer, Nathalie Ollivier, Bérénice Leclercq, Hervé Drobecq, Jérôme Vicogne, Vangelis Agouridas () and Oleg Melnyk ()
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Vincent Diemer: U1019-UMR 9017-CIIL-Center for Infection and Immunity of Lille
Nathalie Ollivier: U1019-UMR 9017-CIIL-Center for Infection and Immunity of Lille
Bérénice Leclercq: U1019-UMR 9017-CIIL-Center for Infection and Immunity of Lille
Hervé Drobecq: U1019-UMR 9017-CIIL-Center for Infection and Immunity of Lille
Jérôme Vicogne: U1019-UMR 9017-CIIL-Center for Infection and Immunity of Lille
Vangelis Agouridas: U1019-UMR 9017-CIIL-Center for Infection and Immunity of Lille
Oleg Melnyk: U1019-UMR 9017-CIIL-Center for Infection and Immunity of Lille

Nature Communications, 2020, vol. 11, issue 1, 1-14

Abstract: Abstract The control of cysteine reactivity is of paramount importance for the synthesis of proteins using the native chemical ligation (NCL) reaction. We report that this goal can be achieved in a traceless manner during ligation by appending a simple N-selenoethyl group to cysteine. While in synthetic organic chemistry the cleavage of carbon-nitrogen bonds is notoriously difficult, we describe that N-selenoethyl cysteine (SetCys) loses its selenoethyl arm in water under mild conditions upon reduction of its selenosulfide bond. Detailed mechanistic investigations show that the cleavage of the selenoethyl arm proceeds through an anionic mechanism with assistance of the cysteine thiol group. The implementation of the SetCys unit in a process enabling the modular and straightforward assembly of linear or backbone cyclized polypeptides is illustrated by the synthesis of biologically active cyclic hepatocyte growth factor variants.

Date: 2020
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DOI: 10.1038/s41467-020-16359-6

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