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Galectin inhibitors target galectins, animal lectins that bind β-galactoside sugars on glycoproteins. Each galectin carries at least one conserved carbohydrate recognition domain (CRD), which recognizes lactose and N-acetyllactosamine units in glycans. By cross-linking glycoproteins, galectins influence cell adhesion, immune cell signaling, fibrosis and tumor progression. Galectin-1 and galectin-3 are the family members most studied with small molecules. Many inhibitors mimic the natural sugar ligands, from the disaccharide thiodigalactoside to synthetic galectin-3 ligands such as GB1107 and selvigaltin. Belapectin is a complex plant-derived polysaccharide studied as a galectin-3 inhibitor. OTX008, a calixarene derivative, is listed as a galectin-1 inhibitor.
Galectin-8-IN-1 is a selective ligand targeting the N-terminal domain of galectin-8 (galectin-8N), exhibiting a dissociation constant (Kd) of 48 μM. This compound demonstrates a 15-fold selectivity over galectin-3, as well as significantly enhanced selectivity against other mammalian galectins. Galectin-8-IN-1 is valuable for research applications focused on galectin biology, immune responses, and cell signaling pathways.
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