Current Research in Bioinformatics

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

Nesrine Sadaoui-Smadhi, Souad Khemili-Talbi, Wadood Abdul, Souheyla Toubal, Wafa Mokhtari, Narimen Benhabyles, Karim Arab, Khettal Bachra and Rahim Fazal

DOI : 10.3844/ajbsp.2019.42.45

Current Research in Bioinformatics

Volume 8, 2019

Pages 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.

Copyright

© 2019 Nesrine Sadaoui-Smadhi, Souad Khemili-Talbi, Wadood Abdul, Souheyla Toubal, Wafa Mokhtari, Narimen Benhabyles, Karim Arab, Khettal Bachra and Rahim Fazal. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.