Search

The inhibition activities and mechanisms of four anthocyanins including cyanidin-3-glucoside, cyanidin-3,5-glucoside, cyanidin-3-rutinoside, and peonidin-3-glucoside, against porcine pancreatic α-amylase were investigated through in vitro and in silico studies. The in vitro inhibition study demonstrated that the four anthocyanins competitively inhibited porcine pancreatic α-amylase, which was later verified by the in silico molecular docking study that showed all the anthocyanins bound exclusively to the active site of porcine pancreatic α-amylase. Cyanidin-3-glucoside was found to have the highest inhibition activity with the Ki value of 0.014 mM, followed by cyanidin-3-rutinoside, cyanidin-3,5-glucoside, and peonidin-3-glucoside with the Ki value of 0.019, 0.020, and 0.045 mM, respectively. Results obtained from the in silico study also showed that the four anthocyanins were surrounded by the side chains of the active site of porcine pancreatic α-amylase, among which the side chain of GLU233 was supposed to play a key role in imparting the inhibition activity of anthocyanins.

A simple and efficient synthesis of novel estrone 16α,17α-oxazoline derivatives substituted at the D ring (compounds 6a-g) is described. The reduction of 16α-azido-3-methoxyestra-1,3,5-trien-17-one (1) in methanol in the presence of CeCl 3 under the condition of the Luche reaction produced two epimeric azido alcohol (16α-azido-17α-hydroxy and 16α-azido-17β-hydroxy) derivatives of estra-1,3,5(10)-triene-3-methyl ether (compounds 2 and 3) in a yield of 90% and 7.6%. The reaction of the sterically unhindered 16α-azido-17α-hydroxy-estra-1,3,5(10)-triene-3-methyl ether (2) with a range of benzaldehydes under the condition of the Schmidt rearrangement yielded d-ring substituted estrone 16α,17α-oxazoline derivatives 6a-g. The in vitro antiproliferative activities of compounds 1, 2, 3, 6a-g were also determined by means of MTT assays on a panel of human cancer cell lines HeLa, SiHa, C-33 A, A2780, MCF-7, MDA-MB-231 and T47D., (Copyright © 2021. Published by Elsevier Inc.)

Based on the presence of carbamate moiety, twenty salicylanilide N-monosubstituted carbamates concomitantly with their parent salicylanilides and five newly prepared 4-chlorophenyl carbamates obtained from isocyanates were investigated using Ellman's method for their in vitro inhibitory activity against acetylcholinesterase (AChE) from electric eel and butyrylcholinesterase (BChE) from equine serum. The carbamates and salicylanilides exhibited mostly a moderate inhibition of both cholinesterase enzymes with IC 50 values ranging from 5 to 235 µM. IC 50 values for AChE were in a narrower concentration range when compared to BChE, but many of the compounds produced a balanced inhibition of both cholinesterases. The derivatives were comparable or superior to rivastigmine for AChE inhibition, but only a few of carbamates also for BChE. Several structure-activity relationships were identified, e.g., N-phenethylcarbamates produce clearly favourable BChE inhibition. The compounds also share convenient physicochemical properties for CNS penetration., (Copyright © 2018 Elsevier Inc. All rights reserved.)