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Abstract
Aim:
There is little information available on the monoamine oxidase isoform selectivity
of
N-alkyl harmine analogs, which exhibit a myriad of activities including MAO-A, DYRK1A
and cytotoxicity to several select cancer cell lines.
Results:
Compounds
3e and
4c exhibited an IC
50 of 0.83 ± 0.03 and 0.43 ± 0.002 μM against MAO-A and an IC
50 of 0.26 ± 0.04 and 0.36 ± 0.001 μM against MAO-B, respectively. Molecular docking
studies revealed π–π interactions between the synthesized molecules and aromatic amino
acid residues.
Conclusion & future perspective:
The current study delineates the structural requirements for MAO-A selectivity and
such information may be helpful in designing selective analogs for kinase, DYRK1A
and harmine-based cytotoxics without apparent MAO enzyme inhibition.
[1
]National Center for Natural Products Research, School of Pharmacy, The University
of Mississippi, MS 38677, USA
[2
]Division of Pharmacognosy, Division of Pharmacology, Department of BioMolecular Sciences,
School of Pharmacy, The University of Mississippi, MS 38677, USA