Titre :

Semi-synthesis of a tag-free O-GlcNAcylated tau protein by sequential chemoselective ligation: Semi-Synthesis of a Tag-free O-GlcNAcylated Tau Protein

Auteur(s) :

Schwagerus, Sergej [Auteur]
Leibniz Forschungsinstitut für Molekulare Pharmakolgie = Leibniz Institute for Molecular Pharmacology [Berlin, Allemagne] [FMP]
Reimann, Oliver [Auteur]
Leibniz Forschungsinstitut für Molekulare Pharmakolgie = Leibniz Institute for Molecular Pharmacology [Berlin, Allemagne] [FMP]
Despres, Clément [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Nocca Smet, Caroline [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Hackenberger, Christian P. R. [Auteur]
Leibniz Forschungsinstitut für Molekulare Pharmakolgie = Leibniz Institute for Molecular Pharmacology [Berlin, Allemagne] [FMP]

Titre de la revue :

Journal of Peptide Science

Numéro :

22

Pagination :

327-333

Date de publication :

2016-05

ISSN :

10752617

Mot(s)-clé(s) en anglais :

native chemical ligation
protein synthesis
tag-free purification
tau protein
O-GIcNac

Discipline(s) HAL :

Chimie/Chimie théorique et/ou physique

Résumé en anglais : [en]

In this paper, the first semi‐synthesis of the Alzheimer‐relevant tau protein carrying an O‐GlcNAcylation is demonstrated by using sequential chemoselective ligation. The 52‐amino acid C‐terminus of tau was obtained by ...
Lire la suite >In this paper, the first semi‐synthesis of the Alzheimer‐relevant tau protein carrying an O‐GlcNAcylation is demonstrated by using sequential chemoselective ligation. The 52‐amino acid C‐terminus of tau was obtained by native chemical ligation between two synthetic peptide fragments, one carrying the O‐GlcNAc moiety on Ser400, which has recently been demonstrated to inhibit tau phosphorylation and to hinder tau oligomerization, and the other equipped with a photocleavable biotin handle. After desulfurization to deliver a native alanine at the ligation junction, the N‐terminal cysteine was unmasked, and the peptide was further used for expressed protein ligation to generate the full‐length tau protein, which was purified by a photocleavable biotin tag. We thus provide a synthetic route to obtain a homogenous tag‐free O‐GlcNAcylated tau protein that can further help to elucidate the significance of posttranslational modification on the tau protein and pave the way for evaluating possible drug targets in Alzheimer's disease.Lire moins >

Langue :

Anglais

Audience :

Non spécifiée

Projet ANR :

Développement de stratégies innovantes pour une approche transdisciplinaire de la maladie d'Alzheime

Établissement(s) :

CNRS
Université de Lille

Collections :

• Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576

Équipe(s) de recherche :

RMN et interactions moléculaires

Date de dépôt :

2020-02-12T15:44:52Z
2021-04-28T06:26:42Z