Marco Catto

TL;DR: A set of 17 coumarin and 2 chromone derivatives with known inhibitory activity toward monoamine oxidase A and B were tested as acetylcholinesterase (AChE) inhibitors and showed that most compounds acted as noncompetitive AChE inhibitors.

TL;DR: A large series of coumarin derivatives were tested for their monoamine oxidase A and B inhibitory activity, revealing the importance of lipophilic interactions in modulating the inhibition and excluding any dependence on electronic properties.

TL;DR: Structural-affinity and structure-selectivity relationships, derived through CoMFA-GOLPE and docking studies, revealed the key physicochemical interactions responsible for the observed MAO-B andMAO-A inhibitory potency and suggested the main structural determinants for high selectivity toward one of the two enzymatic isoforms.

TL;DR: The pyrimidine derivatives proved to be reversible and selective MAO-A inhibitors, and structure-activity relations highlighted the main factors determining both selectivity and inhibitory potency.

TL;DR: The impact of species-dependent differences between human and rat MAO B on inhibitor screening was evidenced for two classes of compounds, coumarin and 5H-indeno[1,2-c]pyridazin-5-one derivatives, suggesting different binding modes.