Synthesis and evaluation of fructose analogues as inhibitors of the D-fructose transporter GLUT5

A Tatibouet, J Yang, C Morin, G D Holman

Research output: Contribution to journalArticle

31 Citations (Scopus)

Abstract

We have examined the specificity and binding-site spatial requirements of the fructose transporter GLUT5. Interaction with a series of fructofuranosides and fructopyranosides suggests that both furanose and pyranose ring forms of D-fructose combine with GLUT5. The epimers of D-fructose all have low affinity for GLUT5 suggesting that the transporter requires all hydroxyls to be in the fructo-configuration. Similarly there is poor tolerance of all allyl derivatives of D-fructose except 6-O-allyl-D-fructo-furanose. Therefore, the C-6 position offers the most suitable position for development of affinity probes and labels for exploring GLUT5 biochemistry. (C) 2000 Elsevier Science Ltd. All rights reserved.
Original languageEnglish
Pages (from-to)1825-1833
Number of pages9
JournalBioorganic and Medicinal Chemistry
Volume8
Issue number7
Publication statusPublished - 2000

Fingerprint

biochemistry
inhibitor
tolerance
probe
evaluation

Cite this

Synthesis and evaluation of fructose analogues as inhibitors of the D-fructose transporter GLUT5. / Tatibouet, A; Yang, J; Morin, C; Holman, G D.

In: Bioorganic and Medicinal Chemistry, Vol. 8, No. 7, 2000, p. 1825-1833.

Research output: Contribution to journalArticle

@article{15fdee206b234896956a03fa247da83b,
title = "Synthesis and evaluation of fructose analogues as inhibitors of the D-fructose transporter GLUT5",
abstract = "We have examined the specificity and binding-site spatial requirements of the fructose transporter GLUT5. Interaction with a series of fructofuranosides and fructopyranosides suggests that both furanose and pyranose ring forms of D-fructose combine with GLUT5. The epimers of D-fructose all have low affinity for GLUT5 suggesting that the transporter requires all hydroxyls to be in the fructo-configuration. Similarly there is poor tolerance of all allyl derivatives of D-fructose except 6-O-allyl-D-fructo-furanose. Therefore, the C-6 position offers the most suitable position for development of affinity probes and labels for exploring GLUT5 biochemistry. (C) 2000 Elsevier Science Ltd. All rights reserved.",
author = "A Tatibouet and J Yang and C Morin and Holman, {G D}",
note = "ID number: ISI:000088281900031",
year = "2000",
language = "English",
volume = "8",
pages = "1825--1833",
journal = "Bioorganic and Medicinal Chemistry",
issn = "0968-0896",
publisher = "Elsevier",
number = "7",

}

TY - JOUR

T1 - Synthesis and evaluation of fructose analogues as inhibitors of the D-fructose transporter GLUT5

AU - Tatibouet, A

AU - Yang, J

AU - Morin, C

AU - Holman, G D

N1 - ID number: ISI:000088281900031

PY - 2000

Y1 - 2000

N2 - We have examined the specificity and binding-site spatial requirements of the fructose transporter GLUT5. Interaction with a series of fructofuranosides and fructopyranosides suggests that both furanose and pyranose ring forms of D-fructose combine with GLUT5. The epimers of D-fructose all have low affinity for GLUT5 suggesting that the transporter requires all hydroxyls to be in the fructo-configuration. Similarly there is poor tolerance of all allyl derivatives of D-fructose except 6-O-allyl-D-fructo-furanose. Therefore, the C-6 position offers the most suitable position for development of affinity probes and labels for exploring GLUT5 biochemistry. (C) 2000 Elsevier Science Ltd. All rights reserved.

AB - We have examined the specificity and binding-site spatial requirements of the fructose transporter GLUT5. Interaction with a series of fructofuranosides and fructopyranosides suggests that both furanose and pyranose ring forms of D-fructose combine with GLUT5. The epimers of D-fructose all have low affinity for GLUT5 suggesting that the transporter requires all hydroxyls to be in the fructo-configuration. Similarly there is poor tolerance of all allyl derivatives of D-fructose except 6-O-allyl-D-fructo-furanose. Therefore, the C-6 position offers the most suitable position for development of affinity probes and labels for exploring GLUT5 biochemistry. (C) 2000 Elsevier Science Ltd. All rights reserved.

M3 - Article

VL - 8

SP - 1825

EP - 1833

JO - Bioorganic and Medicinal Chemistry

JF - Bioorganic and Medicinal Chemistry

SN - 0968-0896

IS - 7

ER -