Titre :

Engineered oxalyl thioester-containing protein domains as a building block for synthetic biopolymers

Auteur(s) :

Terzani, Francesco [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Rostami, Simindokht [Auteur]
Universität für Bodenkultur Wien = University of Natural Resources and Life Sciences [Vienne, Autriche] [BOKU]
Wang, Chen [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]
Wiltschi, Birgit [Auteur]
Universität für Bodenkultur Wien = University of Natural Resources and Life Sciences [Vienne, Autriche] [BOKU]
Melnyk, Oleg [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Agouridas, Vangelis [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]

Titre de la manifestation scientifique :

Non canonical amino acids : tools for biological and biophysical investigations

Ville :

Paris

Pays :

France

Date de début de la manifestation scientifique :

2024-10-14

Discipline(s) HAL :

Chimie

Résumé en anglais : [en]

In recent years, the production of genetically engineered protein biopolymers has been the subject of intense research with promising applications in biomedical or materials science.1 Despite significant advances, the ...
Lire la suite >In recent years, the production of genetically engineered protein biopolymers has been the subject of intense research with promising applications in biomedical or materials science.1 Despite significant advances, the access to tailored biopolymers and thus, the development of versatile and efficient approaches, remain major challenges. We recently documented the potential of oxalyl thioester precursors (oxoSEA) as reactive handles for the modification of peptides and proteins.2,3 Upon activation by a reductant, they can react in an NCL-fashion4 with an N-terminal cysteine residue to provide a ligated peptide. Notably, the reaction has been reported to be highly chemoselective, triggered on-demand, fast (< 30 M-1 s-1) and efficient in the high nanomolar range. The goal of this project is to build on the tremendous reactivity of oxalyl thioesters in order to access high-molecular weight biopolymers by polycondensation of bifunctional protein-derived monomers. This will be done by setting up a fully integrated approach from synthetic biology to chemistry, involving the recombinant production of monomeric units equipped with an N-terminal cysteine residue and a genetically encoded oxoSEA-amino acid derivative close to the C-terminus.Lire moins >

Langue :

Anglais

Comité de lecture :

Oui

Audience :

Internationale

Vulgarisation :

Non

Collections :

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

Source :

Harvested from HAL

Date de dépôt :

2025-01-22T09:55:25Z