BindingDB Entry 50032703: β-Carboline Derivatives as Monoamine Oxidase Inhibitors

BindingDB entry 50032703, sourced from a paper by the University of Namur, describes synthesized β-carboline derivatives evaluated as inhibitors of human monoamine oxidase A and B. The dataset likely contains measured Ki values for each compound, including the most active MAO-A inhibitor with a Ki of 3.6 nM and the best MAO-B inhibitor with a Ki of 221.6 nM. Molecular docking studies suggest how specific lipophilic groups occupy hydrophobic pockets in the enzymes.

Use Cases

• Train quantitative structure-activity relationship (QSAR) models based on Ki values for MAO-A and MAO-B inhibition.
• Validate molecular docking poses based on described hydrophobic pocket occupancy for specific O-alkylated chains.
• Screen for selective MAO-A inhibitors based on the reported activity differences between MAO-A and MAO-B for O-alkylated compounds.
• Analyze structure-activity trends for β-carboline scaffolds based on the described effects of lipophilic groups like cyclohexyl and trifluorobutyloxy.

Strengths

• Includes specific, quantitative Ki values for enzyme inhibition, such as 3.6 nM for the most active MAO-A inhibitor.
• Provides a clear biological rationale for compound design based on a described hydrophobic pocket in the MAO-A crystal structure.
• Compares inhibitory activity against two related enzyme targets, MAO-A and MAO-B, for the synthesized series.

Limitations

• Column-level documentation is absent; field semantics must be inferred after download.
• Row count is unknown, which may limit suitability assessment.
• Last update date is unknown; freshness unverified.

Provenance

Source

University of Namur via BindingDB and paperswithcode

Collection Method

Experimental synthesis and biochemical evaluation described in a scientific paper.