Bioorganic & medicinal chemistry

Inhibition of monoamine oxidase by selected C5-and C6-substituted isatin analogues

CI Manley-King, JJ Bergh, JP Petzer

Index: Manley-King, Clarina I.; Bergh, Jacobus J.; Petzer, Jacobus P. Bioorganic and Medicinal Chemistry, 2011 , vol. 19, # 1 p. 261 - 274

Full Text: HTML

Citation Number: 59

Abstract

Previous studies have shown that (E)-5-styrylisatin and (E)-6-styrylisatin are reversible inhibitors of human monoamine oxidase (MAO) A and B. Both homologues are reported to exhibit selective binding to the MAO-B isoform with (E)-5-styrylisatin being the most potent inhibitor. To further investigate these structure–activity relationships (SAR), in the present study, additional C5-and C6-substituted isatin analogues were synthesized and evaluated ...