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dc.contributor.authorMostert, Samantha
dc.contributor.authorPetzer, Anél
dc.contributor.authorPetzer, Jacobus P.
dc.date.accessioned2016-10-31T09:25:03Z
dc.date.available2016-10-31T09:25:03Z
dc.date.issued2016
dc.identifier.citationMostert, S. et al. 2016. Evaluation of natural and synthetic 1,4-naphthoquinones as inhibitors of monoamine oxidase. Chemical biology and drug design, 87(5):737-746. [https://doi.org/10.1111/cbdd.12708]en_US
dc.identifier.issn1747-0277
dc.identifier.issn1747-0285 (Online)
dc.identifier.urihttp://hdl.handle.net/10394/19239
dc.identifier.urihttps://doi.org/10.1111/cbdd.12708
dc.identifier.urihttps://onlinelibrary.wiley.com/doi/abs/10.1111/cbdd.12708
dc.description.abstractPrevious reports have documented that 1,4-naphtho- quinones act as inhibitors of the monoamine oxidase (MAO) enzymes. In particular, fractionation of the extracts of cured tobacco leafs has led to the charac- terization of 2,3,6-trimethyl-1,4-naphthoquinone, a non- selective MAO inhibitor. To derive structure–activity relationships for MAO inhibition by the 1,4-naphthoqui- none class of compounds, this study investigates the human MAO inhibitory activities of fourteen structurally diverse 1,4-naphthoquinones of natural and synthetic origin. Of these, 5,8-dihydroxy-1,4-naphthoquinone was found to be the most potent inhibitor with an IC 50 value of 0.860 l M for the inhibition of MAO-B. A related compound, shikonin, inhibits both the MAO-A and MAO-B isoforms with IC 50 values of 1.50 and 1.01 lM, respectively. It is further shown that MAO-A and MAO- B inhibition by these compounds is reversible by dialy- sis. In this respect, kinetic analysis suggests that the modes of MAO inhibition are competitive. This study contributes to the discovery of novel MAO inhibitors, which may be useful in the treatment for disorders such as Parkinson’s disease, depressive illness, con- gestive heart failure and canceren_US
dc.language.isoenen_US
dc.publisherWileyen_US
dc.subject1,4-Naphthoquinoneen_US
dc.subjectCompetitiveen_US
dc.subjectDialysisen_US
dc.subjectInhibitionen_US
dc.subjectMonoamine oxidaseen_US
dc.subjectReversibleen_US
dc.titleEvaluation of natural and synthetic 1,4-naphthoquinones as inhibitors of monoamine oxidaseen_US
dc.typeArticleen_US
dc.contributor.researchID12264954 - Petzer, Anél
dc.contributor.researchID10727388 - Petzer, Jacobus Petrus
dc.contributor.researchID20574991 - Mostert, Samantha


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