Carbocisteine exhibits a diverse range of pharmacological activities. It acts as an inhibitor of the Eg5 protein by inhibiting ATP hydrolysis with an IC50 greater than 63,000 nM, and demonstrates cytotoxic activity against HeLa cells with an IC50 greater than 50,000 nM. In terms of enzyme inhibition, the compound shows no activity against human recombinant UGT1A6 and UGT1A9 enzymes.
Moderate liver toxicity is observed, indicated by elevated ALT or AST serum activity during clinical trials, although it does not cause acute liver toxicity or other specific forms of severe liver damage. Besides its weak antiviral activity against SARS-CoV-2, with a notable inhibition rate of 0.3% at 10 µM concentrations for 48 hours in Caco-2 cells and varied inhibition percentages in VERO-6 cells and 3CL-Pro protease assays, the compound also demonstrates potential inhibition of HDAC6, with enzymatic assay inhibition percentages of 17.77% and 12.71% using different substrates.
Moreover, Carbocisteine shows significant binding affinities and modulatory activities toward various neurotransmitter receptors and enzymes. This includes binding to ADRB1, ADRB2, SLC6A3, CHRNA4, HTR2C, DRD2, ADORA1, ADORA3, among others, and displaying agonistic activity at OPRM1 and DRD1 receptors, while acting antagonistically at CHRM2, HTR1A, ADRA1A, NR1I2, HTR2A, HTR2B, CNR1, rat Ar receptors, and inhibiting enzymes like PDE4D, PDE3A, MAOA, and Ptgs1.
These interactions suggest that Carbocisteine has potential bioactivity related to neurotransmitter modulation, enzyme inhibition, and antiviral effects, warranting further research into its pharmacological applications..
Note: Summary generated by AI. Data source: ChEMBL 