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

Research output: Contribution to journal › Article › peer-review

Abstract

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.

Original language	English
Pages (from-to)	1472-1484
Number of pages	13
Journal	European Journal of Organic Chemistry
Volume	2015
Issue number	7
DOIs	https://doi.org/10.1002/ejoc.201403363
Publication status	Published - 2015

Keywords

Carbohydrates
Conformation analysis
Enzymes
Inhibitors

Access to Document

10.1002/ejoc.201403363

Cite this

@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

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Physical Chemistry and characterization(PC2)

CCDC 910797: Experimental Crystal Structure Determination

CCDC 910795: Experimental Crystal Structure Determination

CCDC 910796: Experimental Crystal Structure Determination

Cite this

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

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Equipment

Physical Chemistry and characterization(PC2)

Datasets

CCDC 910797: Experimental Crystal Structure Determination

CCDC 910795: Experimental Crystal Structure Determination

CCDC 910796: Experimental Crystal Structure Determination

Cite this