Planta Med 2015; 81 - PW_128
DOI: 10.1055/s-0035-1565752

Inhibitory potential of Rosa canina and Rosa sempervirens fruit extracts towards acetylcholinesterase

D Pintać 1, T Majkić 1, J Naðpal 1, Z Mrkonjić 1, K Bekvalac 1, M Lesjak 1, I Beara 1
  • 1Department of Chemistry, Biochemistry and Environmental Protection, Faculty of Sciences, University of Novi Sad, Novi Sad, Serbia

Acetylcholinesterase (AChE) is a key enzyme catalysing the hydrolysis of acetylcholine in the nervous system. The inhibitors of AChE are used in treatment of Alzheimer's disease. Due to numerous side effects of synthetic AChE inhibitors, there is a great need for new inhibitors, preferably from natural sources. Thus, the aim of this study was to examine AChE inhibitory potential of water and methanol fruit extracts of Rosa canina L., traditionally used in folk medicine, and poorly investigated Rosa sempervirens L. The inhibitory effect of the extracts was evaluated using a modified in vitro spectrophotometric Ellman's method [1]. During the method optimization, it was tested how buffers (Tris-HCl and phosphate buffer), frequently used in the assay, and solvents used for plant extract dilution (DMSO, methanol, ethanol, water) affect the enzyme activity. The results suggest that the use of 20 mM Tris-HCl pH 8 as a buffer and water as a solvent had the lowest influence on AChE activity, so they were chosen as optimal. All investigated extracts of R. sempervirens expressed greater activity than those of R. canina. Methanol dry fruit extract of R. sempervirens expressed the highest activity (IC50 = 1.2 mg mL-1), while water fresh fruit extract of R. canina exhibited the lowest AChE inhibitory potential. In comparison with galantamine, a well-known potent inhibitor of AChE but with adverse effects, all extracts manifested weaker activity.

The results obtained indicate that R. sempervirens has good potential for application in treatment of Alzheimer's disease and support further investigation of this poorly investigated species. Additionally, the optimal experimental conditions for successful determination of natural products inhibitory potential towards AChE are defined in this study.

References:

[1] Ellman GL, Courtney KD, Andres V, Featherstone RM. A new and rapid colorimetric determination of acetylcholinesterase activity. Biochem Pharmacol 1961; 7: 88 – 95