Stereoselective synthesis of boat-locked glycosides designed as glycosyl hydrolase conformational probes

Emilie Thiery; Jérémy Reniers; Johan Wouters; Stéphane P. Vincent

doi:10.1002/ejoc.201403363

Stereoselective synthesis of boat-locked glycosides designed as glycosyl hydrolase conformational probes

Emilie Thiery, Jérémy Reniers, Johan Wouters, Stéphane P. Vincent

Résultats de recherche: Contribution à un journal/une revue › Article › Revue par des pairs

Résumé

A general method for the preparation of galactose derivatives locked in a <sup>1,4</sup>B boat conformation has been developed. The boat scaffold was stereoselectively functionalized at the C-1′ position by aliphatic and aromatic groups along with azido or hydroxy groups. The configuration at the new stereogenic center was controlled and determined by X-raydiffraction. These molecules were designed to probe the conformational itinerary of the substrate of glycosyl hydrolases. Inhibition assays were performed against a series of commercially available glycosidases, which showed that these enzymes do not harness a <sup>1,4</sup>B-boat-like transition state.

langue originale	Anglais
Pages (de - à)	1472-1484
Nombre de pages	13
journal	European Journal of Organic Chemistry
Volume	2015
Numéro de publication	7
Les DOIs	https://doi.org/10.1002/ejoc.201403363
Etat de la publication	Publié - 2015

Accès au document

10.1002/ejoc.201403363

Autres fichiers et liens

Link to publication in Scopus

Physico-chimie et caractérisation (PC2)
Wouters, J. (!!Manager), Aprile, C. (!!Manager) & Fusaro, L. (!!Manager)
Plateforme technologique Caracterisation physico-chimiques
Equipement/installations: Plateforme technolgique

CCDC 910796: Experimental Crystal Structure Determination
Reniers, J. (Contributeur), Thiery, É. (Contributeur), Vincent, S. (Contributeur) & Wouters, J. (Contributeur), Cambridge Crystallographic Data Centre, 1 janv. 2015
DOI: 10.5517/cczkrjs, http://www.ccdc.cam.ac.uk/services/structure_request?id=doi:10.5517/cczkrjs&sid=DataCite
Ensemble de données
CCDC 910795: Experimental Crystal Structure Determination
Reniers, J. (Contributeur), Thiery, É. (Contributeur), Vincent, S. (Contributeur) & Wouters, J. (Contributeur), Cambridge Crystallographic Data Centre, 1 janv. 2015
DOI: 10.5517/cczkrhr, http://www.ccdc.cam.ac.uk/services/structure_request?id=doi:10.5517/cczkrhr&sid=DataCite
Ensemble de données
CCDC 910797: Experimental Crystal Structure Determination
Reniers, J. (Contributeur), Thiery, É. (Contributeur), Vincent, S. (Contributeur) & Wouters, J. (Contributeur), Cambridge Crystallographic Data Centre, 1 janv. 2015
DOI: 10.5517/cczkrkt, http://www.ccdc.cam.ac.uk/services/structure_request?id=doi:10.5517/cczkrkt&sid=DataCite
Ensemble de données

Contient cette citation

@article{bc73b1b5426f4b2e91e54cef03fa8835,

title = "Stereoselective synthesis of boat-locked glycosides designed as glycosyl hydrolase conformational probes",

abstract = "A general method for the preparation of galactose derivatives locked in a 1,4B boat conformation has been developed. The boat scaffold was stereoselectively functionalized at the C-1′ position by aliphatic and aromatic groups along with azido or hydroxy groups. The configuration at the new stereogenic center was controlled and determined by X-raydiffraction. These molecules were designed to probe the conformational itinerary of the substrate of glycosyl hydrolases. Inhibition assays were performed against a series of commercially available glycosidases, which showed that these enzymes do not harness a 1,4B-boat-like transition state.",

keywords = "Carbohydrates, Conformation analysis, Enzymes, Inhibitors",

author = "Emilie Thiery and J{\'e}r{\'e}my Reniers and Johan Wouters and Vincent, {St{\'e}phane P.}",

year = "2015",

doi = "10.1002/ejoc.201403363",

language = "English",

volume = "2015",

pages = "1472--1484",

journal = "European Journal of Organic Chemistry",

issn = "1434-193X",

publisher = "Wiley-VCH Verlag",

number = "7",

}

TY - JOUR

T1 - Stereoselective synthesis of boat-locked glycosides designed as glycosyl hydrolase conformational probes

AU - Thiery, Emilie

AU - Reniers, Jérémy

AU - Wouters, Johan

AU - Vincent, Stéphane P.

PY - 2015

Y1 - 2015

N2 - A general method for the preparation of galactose derivatives locked in a 1,4B boat conformation has been developed. The boat scaffold was stereoselectively functionalized at the C-1′ position by aliphatic and aromatic groups along with azido or hydroxy groups. The configuration at the new stereogenic center was controlled and determined by X-raydiffraction. These molecules were designed to probe the conformational itinerary of the substrate of glycosyl hydrolases. Inhibition assays were performed against a series of commercially available glycosidases, which showed that these enzymes do not harness a 1,4B-boat-like transition state.

AB - A general method for the preparation of galactose derivatives locked in a 1,4B boat conformation has been developed. The boat scaffold was stereoselectively functionalized at the C-1′ position by aliphatic and aromatic groups along with azido or hydroxy groups. The configuration at the new stereogenic center was controlled and determined by X-raydiffraction. These molecules were designed to probe the conformational itinerary of the substrate of glycosyl hydrolases. Inhibition assays were performed against a series of commercially available glycosidases, which showed that these enzymes do not harness a 1,4B-boat-like transition state.

KW - Carbohydrates

KW - Conformation analysis

KW - Enzymes

KW - Inhibitors

UR - http://www.scopus.com/inward/record.url?scp=84923228190&partnerID=8YFLogxK

U2 - 10.1002/ejoc.201403363

DO - 10.1002/ejoc.201403363

M3 - Article

SN - 1434-193X

VL - 2015

SP - 1472

EP - 1484

JO - European Journal of Organic Chemistry

JF - European Journal of Organic Chemistry

IS - 7

ER -

Stereoselective synthesis of boat-locked glycosides designed as glycosyl hydrolase conformational probes

Résumé

Accès au document

Autres fichiers et liens

Empreinte digitale

Équipement

Physico-chimie et caractérisation (PC2)

Ensembles de données

CCDC 910796: Experimental Crystal Structure Determination

CCDC 910795: Experimental Crystal Structure Determination

CCDC 910797: Experimental Crystal Structure Determination

Contient cette citation