Protein subtype-targeting through ligand epimerization: talose-selectivity of galectin-4 and galectin-8.

Christopher Öberg; Helen Blanchard; Hakon Leffler; Ulf Nilsson

doi:10.1016/j.bmcl.2008.05.066

Protein subtype-targeting through ligand epimerization: talose-selectivity of galectin-4 and galectin-8.

Christopher Öberg, Helen Blanchard, Hakon Leffler, Ulf Nilsson

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

Abstract

A series of O2 and O3-derivatized methyl beta-d-talopyranosides were synthesized and evaluated in vitro as inhibitors of the galactose-binding galectin-1, -2, -3, -4 (N- and C-terminal domains), 8 (N-terminal domain), and 9 (N-terminal domain). Galectin-4C and 8N were found to prefer the d-talopyranose configuration to the natural ligand d-galactopyranose configuration. Derivatization at talose O2 and/or O3 provided selective submillimolar inhibitors for these two galectins.

Original language	English
Pages (from-to)	3691-3694
Journal	Bioorganic & Medicinal Chemistry Letters
Volume	18
Issue number	13
DOIs	https://doi.org/10.1016/j.bmcl.2008.05.066
Publication status	Published - 2008

Bibliographical note

The information about affiliations in this record was updated in December 2015.
The record was previously connected to the following departments: Organic chemistry (S/LTH) (011001240), Division of Microbiology, Immunology and Glycobiology - MIG (013025200)

Subject classification (UKÄ)

Microbiology in the medical area
Immunology in the medical area

Access to Document

10.1016/j.bmcl.2008.05.066

http://www.ncbi.nlm.nih.gov/pubmed/18539029?dopt=Abstract

Cite this

@article{03fbe0d6ecf04fd18da03c2fc4aef9c5,

title = "Protein subtype-targeting through ligand epimerization: talose-selectivity of galectin-4 and galectin-8.",

abstract = "A series of O2 and O3-derivatized methyl beta-d-talopyranosides were synthesized and evaluated in vitro as inhibitors of the galactose-binding galectin-1, -2, -3, -4 (N- and C-terminal domains), 8 (N-terminal domain), and 9 (N-terminal domain). Galectin-4C and 8N were found to prefer the d-talopyranose configuration to the natural ligand d-galactopyranose configuration. Derivatization at talose O2 and/or O3 provided selective submillimolar inhibitors for these two galectins.",

author = "Christopher {\"O}berg and Helen Blanchard and Hakon Leffler and Ulf Nilsson",

note = "The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Organic chemistry (S/LTH) (011001240), Division of Microbiology, Immunology and Glycobiology - MIG (013025200)",

year = "2008",

doi = "10.1016/j.bmcl.2008.05.066",

language = "English",

volume = "18",

pages = "3691--3694",

journal = "Bioorganic & Medicinal Chemistry Letters",

issn = "0960-894X",

publisher = "Elsevier",

number = "13",

}

TY - JOUR

T1 - Protein subtype-targeting through ligand epimerization: talose-selectivity of galectin-4 and galectin-8.

AU - Öberg, Christopher

AU - Blanchard, Helen

AU - Leffler, Hakon

AU - Nilsson, Ulf

N1 - The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Organic chemistry (S/LTH) (011001240), Division of Microbiology, Immunology and Glycobiology - MIG (013025200)

PY - 2008

Y1 - 2008

N2 - A series of O2 and O3-derivatized methyl beta-d-talopyranosides were synthesized and evaluated in vitro as inhibitors of the galactose-binding galectin-1, -2, -3, -4 (N- and C-terminal domains), 8 (N-terminal domain), and 9 (N-terminal domain). Galectin-4C and 8N were found to prefer the d-talopyranose configuration to the natural ligand d-galactopyranose configuration. Derivatization at talose O2 and/or O3 provided selective submillimolar inhibitors for these two galectins.

AB - A series of O2 and O3-derivatized methyl beta-d-talopyranosides were synthesized and evaluated in vitro as inhibitors of the galactose-binding galectin-1, -2, -3, -4 (N- and C-terminal domains), 8 (N-terminal domain), and 9 (N-terminal domain). Galectin-4C and 8N were found to prefer the d-talopyranose configuration to the natural ligand d-galactopyranose configuration. Derivatization at talose O2 and/or O3 provided selective submillimolar inhibitors for these two galectins.

U2 - 10.1016/j.bmcl.2008.05.066

DO - 10.1016/j.bmcl.2008.05.066

M3 - Article

C2 - 18539029

SN - 0960-894X

VL - 18

SP - 3691

EP - 3694

JO - Bioorganic & Medicinal Chemistry Letters

JF - Bioorganic & Medicinal Chemistry Letters

IS - 13

ER -

Protein subtype-targeting through ligand epimerization: talose-selectivity of galectin-4 and galectin-8.

Abstract

Bibliographical note

Subject classification (UKÄ)

Access to Document

Fingerprint

Cite this