Research Article Open Access

In Silico Cholinesterase and Monoamine Oxidase Inhibitory Activities of Perillaldehyde and D-Limonene, Main Compounds of Essential Oil of Algerian Ammodaucus leucotrichus

Nesrine Sadaoui-Smadhi1, Souad Khemili-Talbi1, Wadood Abdul2, Souheyla Toubal3, Wafa Mokhtari4, Narimen Benhabyles3, Karim Arab5, Khettal Bachra6 and Rahim Fazal7
  • 1 Université M'hamed Bougara de Boumerdes, Algeria
  • 2 Abdul Wali Khan University, Pakistan
  • 3 Université de Boumerdes, Algeria
  • 4 Université Libre de Bruxelles, Belgium
  • 5 Université de Boumerdes, Algeria
  • 6 Université de Bejaia, Algeria
  • 7 Hazara University, Pakistan
Current Research in Bioinformatics
Volume 8 No. 1, 2019, 42-45

DOI: https://doi.org/10.3844/ajbsp.2019.42.45

Submitted On: 26 December 2019
Published On: 28 February 2020

How to Cite: Sadaoui-Smadhi, N., Khemili-Talbi, S., Abdul, W., Toubal, S., Mokhtari, W., Benhabyles, N., Arab, K., Bachra, K. & Fazal, R. (2019). In Silico Cholinesterase and Monoamine Oxidase Inhibitory Activities of Perillaldehyde and D-Limonene, Main Compounds of Essential Oil of Algerian Ammodaucus leucotrichus. Current Research in Bioinformatics, 8(1), 42-45. https://doi.org/10.3844/ajbsp.2019.42.45

Abstract

In a continuation of our previous work for the exploration of novel enzyme inhibitors, molecular modeling was used to inspect the binding mode of perillaldehyde and D-limonene, the major compounds of essential oil of Algerian Ammodaucus leucotrichus into the active site pocket of cholinesterase (AChE and BuChE) and Monoamine Oxidase (MAO). The molecular docking was carried out using Molecular Operating Environment (MOE) software package. Docking analysis showed that this compounds (perilladehyde and D-limonene) can interact with both the Catalytic Active Site (CAS) of AChE, BuChE and MAO. For D-limonene, molecular docking showed favorable H-phi interaction with catalytic residue of AchE and BuChE. The perillaldehyde showed best interaction profile with BuChE as compared with compound D-Limonene. The best interaction between perilladehyde and monoamine oxidase was also revealed. This paper shows best correlation between the in vitro study and the in silico molecular docking study of anti-cholinesterase and anti-monoamine oxidase activities.

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Keywords

  • Acetylcholinesterase
  • Butyrylcholinesterase
  • Monoamine Oxidase
  • Molecular Docking
  • Perilladehyde
  • D-limonene