Anti-acetylcholinesterase activity potential of Ocimum essential oils in comparison to its chemical profile via GC/MS and chemometrics

3^rd International Conference and Exhibition on Traditional & Alternative Medicine

August 03-05, 2015 Birmingham, UK

Shahira M Ezzat1, Mohamed A Farag1, Maha M Salama1, Mariane G Tadros2 and Rabah A T Serya2

1Cairo University, Egypt 2Ain Shams University, Egypt

Posters-Accepted Abstracts: Altern Integr Med

Abstract :

Ocimum (sweet basil) is a plant of considerable commercial importance in traditional medicine worldwide as well as for the flavor and sweets industry. The goal of this study was to examine Ocimum essential oils anti-acetylcholinesterase activity and to correlate the activity with their chemical profiles using a metabolome based GC-MS approach coupled to chemometrics. Further, molecular docking was adopted to rationalize for activity found in most active essential oil isolates. Essential oil prepared from 4 species including O. basilicum, O. africanum, O. americanum and O. minimum exhibited significant inhibitory activity with an IC50 values (0.22, 0.175, 0.57, 0.152 mg/ml) respectively comparable to that of physostigmine with an IC50 value of (0.27 mg/ml). Monoterpene hydrocarbons constituted the most dominant chemical group among Ocimum oils: O. basilicum 60.8%, O. africanum 90.5%, O. americanum 95.4% and O. minimum 41.7%, with camphor amounting for ca. 50% in O. africanum and O. americanum, respectively. Monoterprenoid-derived phenolic ethers (i.e. estragole) constituted the most dominant chemical group among O. basilicum and O. minimum, whereas camphor (a ketone) was the most abundant in O. africanum and americanum. Supervised and unsupervised multivariate data analysis clearly separated O. africanum & americanum from other accessions, with estragole, camphor and to less extent �²-linalool contributing for species segregation. Estragole was found the most active AchE inhibitor (IC50 0.05 mg/ ml) followed by cineole (IC50 0.35 mg/ml), eugenol (IC50 6.62 mg/ml) and camphor (IC50 3.263 mg/ml). Molecular docking revealed that these monoterpenoids bind to key amino acids in ACE enzyme catalytic domain similar to well known anticholinesterase drugs i.e., huperzine, physostigmine and aricept and posing them as a novel class of AchE inhibitors.

Biography :

Shahira M Ezzat is a Professor at the Department of Pharmacognosy, Faculty of Pharmacy, Cairo University, Egypt.

Email: shahyelkomy@hotmail.com