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

Öberg, Christopher LU ; Blanchard, Helen ; Leffler, Hakon LU and Nilsson, Ulf LU (2008) In Bioorganic & Medicinal Chemistry Letters 18(13). p.3691-3694
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.
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organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Bioorganic & Medicinal Chemistry Letters
volume
18
issue
13
pages
3691 - 3694
publisher
Elsevier
external identifiers
  • wos:000256708000003
  • pmid:18539029
  • scopus:44749093873
  • pmid:18539029
ISSN
0960-894X
DOI
10.1016/j.bmcl.2008.05.066
language
English
LU publication?
yes
additional info
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)
id
03fbe0d6-ecf0-4fd1-8da0-3c2fc4aef9c5 (old id 1169011)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/18539029?dopt=Abstract
date added to LUP
2016-04-04 09:29:34
date last changed
2022-01-29 18:05:38
@article{03fbe0d6-ecf0-4fd1-8da0-3c2fc4aef9c5,
  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       = {{Öberg, Christopher and Blanchard, Helen and Leffler, Hakon and Nilsson, Ulf}},
  issn         = {{0960-894X}},
  language     = {{eng}},
  number       = {{13}},
  pages        = {{3691--3694}},
  publisher    = {{Elsevier}},
  series       = {{Bioorganic & Medicinal Chemistry Letters}},
  title        = {{Protein subtype-targeting through ligand epimerization: talose-selectivity of galectin-4 and galectin-8.}},
  url          = {{http://dx.doi.org/10.1016/j.bmcl.2008.05.066}},
  doi          = {{10.1016/j.bmcl.2008.05.066}},
  volume       = {{18}},
  year         = {{2008}},
}