A cysteine selenosulfide redox switch for ...
Type de document :
Compte-rendu et recension critique d'ouvrage
Titre :
A cysteine selenosulfide redox switch for protein chemical synthesis
Auteur(s) :
Diemer, Vincent [Auteur]
Institut de biologie de Lille - UMS 3702 [IBL]
Ollivier, Nathalie [Auteur]
Chemical Biology of Flatworms [Lille] [CBF]
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]
Institut de biologie de Lille - UMS 3702 [IBL]
Ollivier, Nathalie [Auteur]
Chemical Biology of Flatworms [Lille] [CBF]
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]
Titre de la revue :
Nature Communications
Pagination :
2558
Éditeur :
Nature Publishing Group
Date de publication :
2020
ISSN :
2041-1723
Discipline(s) HAL :
Chimie/Chimie organique
Chimie/Chimie thérapeutique
Chimie/Chimie thérapeutique
Résumé en anglais : [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 ...
Lire la suite >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.Lire moins >
Lire la suite >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.Lire moins >
Langue :
Anglais
Vulgarisation :
Non
Projet ANR :
Source :
Fichiers
- https://www.nature.com/articles/s41467-020-16359-6.pdf
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- https://hal.archives-ouvertes.fr/hal-02734393/document
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- https://hal.archives-ouvertes.fr/hal-02734393/document
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- A_Cysteine_Selenosulfide_Redox_Switch_for_Protein_Chemical_Synthesis_v2.pdf
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- s41467-020-16359-6.pdf
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