Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2021 Oct 4;26(19):6019.
doi: 10.3390/molecules26196019.

Monoamine Oxidase (MAO) as a Potential Target for Anticancer Drug Design and Development

Reem Aljanabi  1 , Lina Alsous  1 , Dima A Sabbah  2 , Halise Inci Gul  3 , Mustafa Gul  4 , Sanaa K Bardaweel  1
Affiliations
Review

Monoamine Oxidase (MAO) as a Potential Target for Anticancer Drug Design and Development

Reem Aljanabi et al. Molecules. .

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.

Keywords: QSAR; cancer; inhibitors; metastasis; monoamine oxidase; pharmacophore.

PubMed Disclaimer

Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
Oxidation of primary and secondary amines into their respective imine form, followed by nonenzymatic hydrolysis to their corresponding aldehydes or ketones.
Figure 2
Figure 2
Main steps involved in the development of a QSAR model.
Figure 3
Figure 3
Main scaffolds of Xanthone, Pyrrole, Pyridazine, and Phenyl alkylamine derivatives studied as MAO-inhibitors (R1 = OH, R2 = MeO, R3 = MeO, R4 = H or OH R5 = H, R6 = CHMe2, R7 = NHMe, NMe2, NH2, R8 = H).
Figure 4
Figure 4
The structure of pyrrole derivatives; compounds 5 and 6 represent MAO-B and MAO-A selective inhibitors, respectively.
Figure 5
Figure 5
Main scaffolds of indole, isatin, pirlindole, indolylmethyl amine, phenethylamine, and coumarin studied as MAO-inhibitors. (R1 = OH, R2 c = MeO, R3 = MeO, R4 = H or OH R5 = H, R6 = CHMe2, R7 = NHMe, NMe2, NH2).
Figure 6
Figure 6
MAO-A pharmacophore model with (A) 5-((1H-indol-2-yl)methyl) -3-methyl- 2-thioxo imidazolidin -4-one and (B) NSC 38.
Figure 7
Figure 7
Structures of compounds designed employing in silico docking: clorgyline (28), DK382 (29), and fucoxanthin (30).
See this image and copyright information in PMC

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

References

    1. Yeung A.W.K., Georgieva M.G., Atanasov A.G., Tzvetkov N.T. Monoamine oxidases (MAOs) as privileged molecular targets in neuroscience: Research literature analysis. Front. Mol. Neurosci. 2019;19:143. doi: 10.3389/fnmol.2019.00143. - DOI - PMC - PubMed
    1. Tripathi A.C., Upadhyay S., Paliwal S., Saraf S.K. Privileged scaffolds as MAO inhibitors: Retrospect and prospects. Eur. J. Med. Chem. 2018;145:445–497. doi: 10.1016/j.ejmech.2018.01.003. - DOI - PubMed
    1. Manzoor S., Hoda N. A Comprehensive Review of Monoamine Oxidase Inhibitors as Anti-Alzheimer’s Disease Agents: A Review. Eur. J. Med. Chem. 2020;206:112787. doi: 10.1016/j.ejmech.2020.112787. - DOI - PubMed
    1. Shih J.C., Chen K., Ridd M. Monoamine oxidase: From genes to behavior. Ann. Rev. Neurosci. 1999;22:197–217. doi: 10.1146/annurev.neuro.22.1.197. - DOI - PMC - PubMed
    1. Singer T.P., Ramsay R.R. Monoamine oxidases: Old friends hold many surprises. FASEB J. 1995;9:605–610. doi: 10.1096/fasebj.9.8.7768351. - DOI - PubMed

MeSH terms

LinkOut - more resources