Anti-BCHE monoclonal antibody, clone FQS4144(3)

This study aims to compare the anti-diabetic and anti-ageing effect of the Murraya koenigii leaves by using the drying method of convective hot-air drying (40, 50 and 60 degrees C) and two hybrid drying methods through microwave vacuum-drying (6, 9 and 12 W/g) and convective hot-air pre-drying followed by microwave vacuum finishing-drying (50 degrees C followed by 9 W/g), in addition to the freeze-drying, which was used as a control method. The anti-diabetic activity was evaluated by using alpha-amylase and alpha-glucosidase inhibition method, while the anti-ageing activity was measured by using acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) inhibition effect. The results indicated that the dried leaves of M. koenigii were more selective towards alpha-glucosidase inhibition with the percentage ranging from 7.92 to 23.57% at the concentration of 62.52 +/- 22.18 to 20.39 +/- 2.01 mg dried leaves/mL. Concerning the anti-ageing activity, the inhibition effect of AChE was significantly weaker compared to BChE inhibition, revealing that the dried M. koenigii leaves were more selective towards BChE inhibition with the percentage ranged from 79.47 to 87.07%. Furthermore, the Page model and diffusion models showed a good fitting of the model to the empirical data of drying kinetics with the highest coefficient of determination (0.9996; 0.9995) and the lowest values of root-mean-square error (0.0102; 0.0090) and Chi-square coefficients (0.0010; 0.0008). Overall, microwave vacuum-drying is the recommended drying method to be used for M. koenigii leaves due to its promising result obtained for the inhibition of alpha-glucosidase and BChE.

A series of new benzene-based derivatives was designed, synthesized and comprehensively characterized. All of the tested compounds were evaluated for their in vitro ability to potentially inhibit the acetyl- and butyrylcholinesterase enzymes. The selectivity index of individual molecules to cholinesterases was also determined. Generally, the inhibitory potency was stronger against butyryl- compared to acetylcholinesterase; however, some of the compounds showed a promising inhibition of both enzymes. In fact, two compounds (23, benzyl ethyl(1-oxo-1-phenylpropan-2-yl)carbamate and 28, benzyl (1-(3-chlorophenyl)-1-oxopropan-2-yl) (methyl)carbamate) had a very high selectivity index, while the second one (28) reached the lowest inhibitory concentration IC50 value, which corresponds quite well with galanthamine. Moreover, comparative receptor-independent and receptor-dependent structure-activity studies were conducted to explain the observed variations in inhibiting the potential of the investigated carbamate series. The principal objective of the ligand-based study was to comparatively analyze the molecular surface to gain insight into the electronic and/or steric factors that govern the ability to inhibit enzyme activities. The spatial distribution of potentially important steric and electrostatic factors was determined using the probability-guided pharmacophore mapping procedure, which is based on the iterative variable elimination method. Additionally, planar and spatial maps of the host-target interactions were created for all of the active compounds and compared with the drug molecules using the docking methodology.