Lactose-Functionalized Carbosilane Glycodendrimers Are Highly Potent Multivalent Ligands for Galectin-9 Binding: Increased Glycan Affinity to Galectins Correlates with Aggregation Behavior.
Journal
Biomacromolecules
ISSN: 1526-4602
Titre abrégé: Biomacromolecules
Pays: United States
ID NLM: 100892849
Informations de publication
Date de publication:
13 11 2023
13 11 2023
Historique:
medline:
14
11
2023
pubmed:
8
9
2023
entrez:
8
9
2023
Statut:
ppublish
Résumé
Galectins, the glycan binding proteins, and their respective carbohydrate ligands represent a unique fundamental regulatory network modulating a plethora of biological processes. The advances in galectin-targeted therapy must be based on a deep understanding of the mechanism of ligand-protein recognition. Carbosilane dendrimers, the well-defined and finely tunable nanoscaffolds with low toxicity, are promising for multivalent carbohydrate ligand presentation to target galectin receptors. The study discloses a synthetic method for two types of lactose-functionalized carbosilane glycodendrimers (Lac-CS-DDMs). Furthermore, we report their outstanding, dendritic effect-driven affinity to tandem-type galectins, especially Gal-9. In the enzyme-linked immunosorbent assay, the affinity of the third-generation multivalent dendritic ligand bearing 32 lactose units to Gal-9 reached nanomolar values (IC
Identifiants
pubmed: 37680126
doi: 10.1021/acs.biomac.3c00426
pmc: PMC10646984
doi:
Substances chimiques
Lactose
J2B2A4N98G
carbosilane
0
Ligands
0
Galectins
0
Polysaccharides
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
4705-4717Références
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