Anticholinesterase, antioxidant potentials, and molecular docking studies of isolated bioactive compounds from Grewia optiva

• Main Authors: Wasim Ul Bari, Muhammad Zahoor, Alam Zeb, Irfan Khan, Yasir Nazir, Ajmal Khan, Najeeb Ur Rehman, Riaz Ullah, Abdelaat A. Shahat, Hafiz Majid Mahmood
• Format: Article
• Language: English
• Published: Taylor & Francis Group 2019-01-01
• Series: International Journal of Food Properties
• Subjects: β-sitosterol; betulinic acid; dpph; abts; acetyl cholinesterase
• Online Access: http://dx.doi.org/10.1080/10942912.2019.1650763
• ISSN: 1094-2912; 1532-2386

Grewia optiva Drummond ex Burret (Tiliceae) is extensively applied for the treatment of typhoid, diarrhea, malaria, etc., in traditional medication. In this study, four bioactive compounds I (β- sitosterol), II (1, 2, 3 benzene triol), III (7-O-methyl cathachin) and VI (betulinic acid) were isolated from the root of G. optiva. The compounds were characterized through UV, FTIR, NMR, and mass spectroscopic techniques. The isolated compounds were tested for the inhibition of synthetic-free radicals: ABTS and DPPH, and anticholinesterases: AChE and BChE. Compound III demonstrated highest percent free radicals scavenging activities against DPPH and ABTS (86.11 ± 2.20, 85.23 ± 1.61, respectively, for 1000 µg/ml concentrations) with IC50 of 63 µg/ml which were comparable to the IC50 value (35 µg/ml) of ascorbic acid. All isolated compounds also showed excellent inhibitory potential against AChE and BChE. However, β-sitosterol amongst them exhibited highest percent inhibition (87.66 ± 1.93, 85.71 ± 1.17, respectively, at 1000 µg/ml concentration) with IC50 of 62 µg/ml, which was close to the standard galanthamine IC50 values (40 µg/ml). To support the findings of the study silico docking model was applied that predicted possible binding modes of β-sitosterol with AChE and BChE. The para hydroxyl group of the phenolic moiety interacted with the active site water molecule and the side chain carbonyl residues through H-bonding. The remaining part of the active compound packed in a shallow pocket through H-bond.