Robinson, Sarel J.Petzer, Jacobus P.Petzer, AnélBergh, Jacobus J.Lourens, Anna C.U.2015-04-152015-04-152013Robinson, S.J. et al. 2013. Selected furanochalcones as inhibitors of monoamine oxidase. Bioorganic & medicinal chemistry letters, 23(17):4985-4989. [https://doi.org/10.1016/j.bmcl.2013.06.050]0960-894X1464-3405 (Online)http://hdl.handle.net/10394/13691https://www.sciencedirect.com/science/article/pii/S0960894X13007713https://doi.org/10.1016/j.bmcl.2013.06.050The validity of the chalcone scaffold for the design of inhibitors of monoamine oxidase has previously been illustrated. In a systematic attempt to investigate the effect of heterocyclic substitution on the monoamine oxidase inhibitory properties of this versatile scaffold, a series of furanochalcones were synthesized. The results demonstrate that these furan substituted phenylpropenones exhibited moderate to good inhibitory activities towards MAO-B, but showed weak or no inhibition of the MAO-A enzyme. The most active compound, 2E-3-(5-chlorofuran-2-yl)-1-(3-chlorophenyl)prop-2-en-1-one, exhibited an IC50 value of 0.174 lM for the inhibition of MAO-B and 28.6 lM for the inhibition of MAO-A. Interestingly, contrary to data previously reported for chalcones, these furan substituted derivatives acted as reversible inhibitors, while kinetic analysis revealed a competitive mode of bindingenChalconemonoamine oxidaseMAO-BReversible inhibitionCompetitiveArticle