Skip to main content

Lund University Publications

LUND UNIVERSITY LIBRARIES

Fragment-based development of triazole-substituted O-galactosyl aldoximes with fragment-induced affinity and selectivity for galectin-3.

Tejler, Johan LU ; Salameh, Bader ; Leffler, Hakon LU and Nilsson, Ulf LU (2009) In Organic and Biomolecular Chemistry 7(19). p.3982-3990
Abstract
A fragment-based development of 3C-triazol-1-yl-O-galactopyranosyl aldoximes led to the discovery of highly selective and high affinity (K(d) down to 11 microm) small monosaccharide based inhibitors of galectin-3. Galectin-7, 8 N-terminal CRD, and 9 N-terminal CRD bound the inhibitors only weakly. The galectin-3 selectivity was hypothesized to stem from interaction of the aldoxime moiety with a site not present in the other galectins.
Please use this url to cite or link to this publication:
author
; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Organic and Biomolecular Chemistry
volume
7
issue
19
pages
3982 - 3990
publisher
Royal Society of Chemistry
external identifiers
  • wos:000269892900015
  • pmid:19763301
  • scopus:70349281538
ISSN
1477-0539
DOI
10.1039/b909091f
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
2a635acc-a8de-47e0-86cc-690e0cfb0a19 (old id 1483366)
date added to LUP
2016-04-01 11:38:27
date last changed
2022-04-05 02:41:04
@article{2a635acc-a8de-47e0-86cc-690e0cfb0a19,
  abstract     = {{A fragment-based development of 3C-triazol-1-yl-O-galactopyranosyl aldoximes led to the discovery of highly selective and high affinity (K(d) down to 11 microm) small monosaccharide based inhibitors of galectin-3. Galectin-7, 8 N-terminal CRD, and 9 N-terminal CRD bound the inhibitors only weakly. The galectin-3 selectivity was hypothesized to stem from interaction of the aldoxime moiety with a site not present in the other galectins.}},
  author       = {{Tejler, Johan and Salameh, Bader and Leffler, Hakon and Nilsson, Ulf}},
  issn         = {{1477-0539}},
  language     = {{eng}},
  number       = {{19}},
  pages        = {{3982--3990}},
  publisher    = {{Royal Society of Chemistry}},
  series       = {{Organic and Biomolecular Chemistry}},
  title        = {{Fragment-based development of triazole-substituted O-galactosyl aldoximes with fragment-induced affinity and selectivity for galectin-3.}},
  url          = {{http://dx.doi.org/10.1039/b909091f}},
  doi          = {{10.1039/b909091f}},
  volume       = {{7}},
  year         = {{2009}},
}