Fast-SEA ligation: a chemoselective ...
Document type :
Autre communication scientifique (congrès sans actes - poster - séminaire...)
Title :
Fast-SEA ligation: a chemoselective NCL-inspired ligation reaction effective in the nanomolar concentration range
Author(s) :
Grain, Benjamin [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Snella, Benoît [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Vicogne, Jérôme [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Capet, Frédéric [Auteur]
Wiltschi, Birgit [Auteur]
Melnyk, Oleg [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
AGOURIDAS, Vangelis [Auteur]
Centrale Lille
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Snella, Benoît [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Vicogne, Jérôme [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Capet, Frédéric [Auteur]
Wiltschi, Birgit [Auteur]
Melnyk, Oleg [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
AGOURIDAS, Vangelis [Auteur]
Centrale Lille
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Conference title :
GFPP 22 / BPGM 5 Joint Meeting of the French and Belgian Peptides and Proteins Societies
Conference organizers(s) :
GFPP / BPGM
City :
Port-Leucate
Country :
France
Start date of the conference :
2022-05-29
Publication date :
2022-06-13
English keyword(s) :
Latency
N.S-Acyl Shift Systems
Non-Native Ligation
Protein Modification
Thioester
N.S-Acyl Shift Systems
Non-Native Ligation
Protein Modification
Thioester
HAL domain(s) :
Chimie/Chimie organique
English abstract : [en]
We show that latent oxalyl thioester surrogates are a powerful means to modify peptides and proteins in highly dilute conditions in purified aqueous media or in mixtures as complex as cell lysates. Designed to be shelf-stable ...
Show more >We show that latent oxalyl thioester surrogates are a powerful means to modify peptides and proteins in highly dilute conditions in purified aqueous media or in mixtures as complex as cell lysates. Designed to be shelf-stable reagents, they can be activated on demand to enable ligation reactions with peptide concentrations as low as a few hundred nM at rates approaching 30 M-1 s-1.Show less >
Show more >We show that latent oxalyl thioester surrogates are a powerful means to modify peptides and proteins in highly dilute conditions in purified aqueous media or in mixtures as complex as cell lysates. Designed to be shelf-stable reagents, they can be activated on demand to enable ligation reactions with peptide concentrations as low as a few hundred nM at rates approaching 30 M-1 s-1.Show less >
Language :
Anglais
Peer reviewed article :
Non
Audience :
Internationale
Popular science :
Oui
Source :
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- https://hal.archives-ouvertes.fr/hal-03695066/document
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- https://hal.archives-ouvertes.fr/hal-03695066/document
- Open access
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- https://hal.archives-ouvertes.fr/hal-03695066/document
- Open access
- Access the document