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

Résultats de recherche: Contribution à un journal/une revueArticle

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 originaleAnglais
Pages (de - à)1472-1484
Nombre de pages13
journalEuropean Journal of Organic Chemistry
Volume2015
Numéro de publication7
Les DOIs
étatPublié - 2015

Empreinte digitale

glucosides
boats
Boats
Hydrolases
Glycosides
probes
synthesis
galactose
harnesses
Glycoside Hydrolases
Galactose
Scaffolds
Conformations
enzymes
Assays
Derivatives
preparation
Molecules
Substrates
Enzymes

Citer ceci

@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

VL - 2015

SP - 1472

EP - 1484

JO - European Journal of Organic Chemistry

JF - European Journal of Organic Chemistry

SN - 1434-193X

IS - 7

ER -