1H-1,2,3-Triazol-1-yl thiodigalactoside derivatives as high affinity galectin-3 inhibitors
(2010) In Bioorganic & Medicinal Chemistry 18(14). p.5367-5378- Abstract
- Galactose C3-triazole derivatives were synthesized by Cu(I)-catalyzed cycloaddition between acetylenes and galactose C3-azido derivatives. Evaluation against galectin-3, 7, 8N (N-terminal) and 9N (N-terminal) revealed 1,4-disubstituted triazoles to be high-affinity inhibitors of galectin-3 with selectivity over galectin-7, 8N, and 9N. Conformational analysis of 1,4-di-and 1,4,5-tri-substituted galactose C3-triazoles suggested that a triazole C5-substituent interfered sterically with the galectin proteins, which explained their poor affinities compared to the corresponding 1,4-disubstituted triazoles. Introduction of two 1,4-disubstituted triazole moieties onto thiodigalactoside resulted in affinities down to 29 nM for galectin-3. (C) 2010... (More)
- Galactose C3-triazole derivatives were synthesized by Cu(I)-catalyzed cycloaddition between acetylenes and galactose C3-azido derivatives. Evaluation against galectin-3, 7, 8N (N-terminal) and 9N (N-terminal) revealed 1,4-disubstituted triazoles to be high-affinity inhibitors of galectin-3 with selectivity over galectin-7, 8N, and 9N. Conformational analysis of 1,4-di-and 1,4,5-tri-substituted galactose C3-triazoles suggested that a triazole C5-substituent interfered sterically with the galectin proteins, which explained their poor affinities compared to the corresponding 1,4-disubstituted triazoles. Introduction of two 1,4-disubstituted triazole moieties onto thiodigalactoside resulted in affinities down to 29 nM for galectin-3. (C) 2010 Elsevier Ltd. All rights reserved. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1657693
- author
- Salameh, Bader A. ; Cumpstey, Ian LU ; Sundin, Anders LU ; Leffler, Hakon LU and Nilsson, Ulf LU
- organization
- publishing date
- 2010
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Galactose, Inhibition, Triazole, Galectin, Azide
- in
- Bioorganic & Medicinal Chemistry
- volume
- 18
- issue
- 14
- pages
- 5367 - 5378
- publisher
- Elsevier
- external identifiers
-
- wos:000279744700056
- scopus:77955335001
- pmid:20538469
- ISSN
- 0968-0896
- DOI
- 10.1016/j.bmc.2010.05.040
- 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: Division of Microbiology, Immunology and Glycobiology - MIG (013025200), Organic chemistry (S/LTH) (011001240)
- id
- 2c9f5382-d477-432d-8ce3-0ca3cde1acfc (old id 1657693)
- date added to LUP
- 2016-04-01 10:01:56
- date last changed
- 2022-04-12 01:09:27
@article{2c9f5382-d477-432d-8ce3-0ca3cde1acfc,
abstract = {{Galactose C3-triazole derivatives were synthesized by Cu(I)-catalyzed cycloaddition between acetylenes and galactose C3-azido derivatives. Evaluation against galectin-3, 7, 8N (N-terminal) and 9N (N-terminal) revealed 1,4-disubstituted triazoles to be high-affinity inhibitors of galectin-3 with selectivity over galectin-7, 8N, and 9N. Conformational analysis of 1,4-di-and 1,4,5-tri-substituted galactose C3-triazoles suggested that a triazole C5-substituent interfered sterically with the galectin proteins, which explained their poor affinities compared to the corresponding 1,4-disubstituted triazoles. Introduction of two 1,4-disubstituted triazole moieties onto thiodigalactoside resulted in affinities down to 29 nM for galectin-3. (C) 2010 Elsevier Ltd. All rights reserved.}},
author = {{Salameh, Bader A. and Cumpstey, Ian and Sundin, Anders and Leffler, Hakon and Nilsson, Ulf}},
issn = {{0968-0896}},
keywords = {{Galactose; Inhibition; Triazole; Galectin; Azide}},
language = {{eng}},
number = {{14}},
pages = {{5367--5378}},
publisher = {{Elsevier}},
series = {{Bioorganic & Medicinal Chemistry}},
title = {{1H-1,2,3-Triazol-1-yl thiodigalactoside derivatives as high affinity galectin-3 inhibitors}},
url = {{http://dx.doi.org/10.1016/j.bmc.2010.05.040}},
doi = {{10.1016/j.bmc.2010.05.040}},
volume = {{18}},
year = {{2010}},
}