Methyl β-D-Galactopyranoside exhibits diverse bioactivities and binding affinities across various targets. It shows a minimum inhibitory concentration (MIC) of 1,750,000 nM for the inhibition of flocculation against the cell wall galactose-specific yeast lectin (KbCWL) and demonstrates an inhibition constant (Ki) of 3.21 for glycogen phosphorylase b. The compound is also an inhibitor of Epstein-Barr virus antigen activation in Raji cells with efficacy increasing at higher concentrations and has a Ki value of 24,700,000 nM for glycogen phosphorylase inhibition.
Additionally, it acts as an antagonist to several human galectins with varying dissociation constants (Kd): 13,000,000 nM for galectin2, 4,400,000 nM for galectin3, 6,600,000 nM for galectin4N, over 10,000,000 nM for galectin4C, 6,300,000 nM for galectin8N, and 1,200,000 nM for galectin9N. Furthermore, Methyl β-D-Galactopyranoside inhibits Pseudomonas aeruginosa PAO1 adhesion to human A549 cells with a 30% inhibition rate at concentrations of 25 to 2500 µM, and displays binding affinity to Pseudomonas aeruginosa LecA with a Kd of 70,000 nM (IC50) and another reported Kd of 55,700 nM by isothermal titration calorimetry.
The compound also inhibits Escherichia coli Heptosyltransferase I, reducing ADP release by 7% at 1 mM. In bioassays, it has shown potent inhibitory activities against AmpC Beta-Lactamase (3162.3 nM) and ROR gamma transcriptional activity (707.9 nM). Despite these activities, it exhibits very low efficacy in displacing a fluorescent probe from human galectin-1, with a Kd greater than 10,000,000 nM, while showing moderate activity for human recombinant galectin-3 with a Kd of 4,400,000 nM. Thus, Methyl β-D-Galactopyranoside indicates potential in multiple biological pathways and target interactions..
Note: Summary generated by AI. Data source: ChEMBL 