Fragment-based development of triazole-substituted O-galactosyl aldoximes with fragment-induced affinity and selectivity for galectin-3.
(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:
https://lup.lub.lu.se/record/1483366
- author
- Tejler, Johan LU ; Salameh, Bader ; Leffler, Hakon LU and Nilsson, Ulf LU
- organization
- publishing date
- 2009
- 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}}, }