A cysteine selenosulfide redox switch for protein chemical synthesis

Diemer, Vincent; Ollivier, Nathalie; Leclercq, Bérénice; Drobecq, Hervé; Vicogne, Jérôme; Agouridas, Vangelis; Melnyk, Oleg

Document type :

Article dans une revue scientifique: Article original

DOI :

10.1038/s41467-020-16359-6

Title :

A cysteine selenosulfide redox switch for protein chemical synthesis

Author(s) :

Diemer, Vincent [Auteur]

Institut de biologie de Lille - UMS 3702 [IBL]
Ollivier, Nathalie [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Leclercq, Bérénice [Auteur]
Drobecq, Hervé [Auteur]
Institut de biologie de Lille - UMS 3702 [IBL]
Vicogne, Jérôme [Auteur]
Institut de biologie de Lille - UMS 3702 [IBL]
Agouridas, Vangelis [Auteur]

Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Melnyk, Oleg [Auteur]

Institut de biologie de Lille - UMS 3702 [IBL]

Journal title :

Nature Communications

Pages :

2558

Publisher :

Nature Publishing Group

Publication date :

2020

ISSN :

2041-1723

HAL domain(s) :

Chimie/Chimie organique
Chimie/Chimie thérapeutique

English abstract : [en]

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 ...
Show more >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.Show less >

Language :

Anglais

Peer reviewed article :

Oui

Audience :

Internationale

Popular science :

Non

ANR Project :

Cations de Zinc(II) à acidité de Lewis forte et modulable: synthèse et utilisation en catalyse

Collections :

Centre d'Infection et d'Immunité de Lille (CIIL) - U1019 - UMR 9017

Source :

Harvested from HAL

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