Abstract
Monoamine oxidases (MAOs) are oxidative enzymes that catalyze the conversion of biogenic amines into their corresponding aldehydes and ketones through oxidative deamination. Owing to the crucial role of MAOs in maintaining functional levels of neurotransmitters, the implications of its distorted activity have been associated with numerous neurological diseases. Recently, an unanticipated role of MAOs in tumor progression and metastasis has been reported. The chemical inhibition of MAOs might be a valuable therapeutic approach for cancer treatment. In this review, we reported computational approaches exploited in the design and development of selective MAO inhibitors accompanied by their biological activities. Additionally, we generated a pharmacophore model for MAO-A active inhibitors to identify the structural motifs to invoke an activity.
Highlights
By 1928, Mary Bernheim discovered the first enzyme of monoamine oxidase, and it was called tyramine oxidases [1]
Monoamine oxidases (MAOs)-A and monoamine oxidase B (MAO-B) are highly expressed in diverse human cancers
monoamine oxidase A (MAO-A) is expressed in prostate and lung cancer, whereas MAO-B is expressed in gliomas and renal cancer
Summary
By 1928, Mary Bernheim discovered the first enzyme of monoamine oxidase, and it was called tyramine oxidases [1]. It is synthetic drugs that demonstrate anticancer activity; curcumin, a bioactive phytochemical compound that is proposed to work through the inhibition of MAO-A/mTOR/HIF-1α signaling pathways, revealed a reduction in cancer-associated fibroblast-induced invasion and ROS production in prostate cancer [26,27,28]. From this perspective, we review the existing studies on the role of MAO-A and MAO-B in cancer development and progression with a special focus on the design and use of MAO-A inhibitors in cancer chemotherapy
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