Monoamine oxidases inhibitors from Colvillea racemosa: Isolation, biological evaluation, and computational study.

ABSTRACT: Bioassay-guided fractionation and chemical investigation of Colvillea racemosa stems led to identification of two new α, β-dihydroxydihydrochalcones, colveol A (1) and colveol B (2) along with fifteen known compounds. The structures were elucidated via interpretation of spectroscopic data. The absolute configurations of the dihydrochalcones 1 and 2 were assigned by a combination of chemical modification and electronic circular dichroism data. The isolated compounds were evaluated for their inhibition activity toward recombinant human monoamine oxidases (rhMAO-A and -B). Compound 1 demonstrated preferential inhibition against hMAO-A isoenzyme (IC₅₀ 0.62μM, SI_A/B 0.02) while S-naringenin (13) and isoliquiritigein (15) demonstrated preferential hMAO-B inhibition (IC

SUBMITTER: Mohamed EI 

PROVIDER: S-EPMC6326099 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature