Discovery and exploration of monosaccharide linked dimers of galectin-3 inhibitors to target fibrosis

Galectin proteins have been targets of interest in numerous therapeutic areas for some time. Galectin-3 has identified as a target particular because its unique structural characteristics and physiological profile. Recent literature indicates galectin-3 inhibition can decrease myofibroblast activation procollagen expression with the potential to affect progression fibrosis lung, liver kidney. Potential π-stacking interactions between one monosaccharide ligand bound carbohydrate recognition domain protein second different molecule were observed extended crystalline lattice an X-ray crystal structure obtained while studying structure-activity relationship. The direct interaction ligands suggests dimeric inhibitors which bind two molecules simultaneously. This work describes exploration dimers designed further probe these observations explore binding or higher order multimeric assemblies.