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ISSN (Print): 1573-4099
ISSN (Online): 1875-6697

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Research Article

Assessment of Anticholinergic and Antidiabetic Properties of Some Natural and Synthetic Molecules: An In vitro and In silico Approach

Author(s): Veysel Çomaklı*, İmdat Aygül, Rüya Sağlamtaş, Müslüm Kuzu, Ramazan Demirdağ, Hülya Akincioğlu, Şevki Adem and İlhami Gülçin

Volume 20, Issue 5, 2024

Published on: 13 June, 2023

Page: [441 - 451] Pages: 11

DOI: 10.2174/1573409919666230518151414

Price: $65

Abstract

Introduction: This study aimed to determine the in vitro and in silico effects of some natural and synthetic molecules on acetylcholinesterase (AChE), butyrylcholinesterase (BChE) and α-glucosidase enzymes.

Background: Alzheimer's disease (AD) and Type II diabetes mellitus (T2DM) are considered the most important diseases of today’s world. However, the side effects of therapeutic agents used in both diseases limit their use. Therefore, developing drugs with high therapeutic efficacy and better pharmacological profile is important.

Objectives: This study sets out to determine the related enzyme inhibitors used in treating AD and T2DM, considered amongst the most important diseases of today’s world.

Methods: In the current study, the in vitro and in silico effects of dienestrol, hesperetin, Lthyroxine, 3,3',5-Triiodo-L-thyronine (T3) and dobutamine molecules on AChE, BChE and α - glycosidase enzyme activities were investigated.

Results: All the molecules showed an inhibitory effect on the enzymes. The IC50 and Ki values of the L-Thyroxine molecule, which showed the strongest inhibition effect for the AChE enzyme, were determined as 1.71 μM and 0.83 ± 0.195 μM, respectively. In addition, dienestrol, T3, and dobutamine molecules showed a more substantial inhibition effect than tacrine. The dobutamine molecule showed the most substantial inhibition effect for the BChE enzyme, and IC50 and Ki values were determined as 1.83 μM and 0.845 ± 0.143 μM, respectively. The IC50 and Ki values for the hesperetin molecule, which showed the strongest inhibition for the α -glycosidase enzyme, were determined as 13.57 μM and 12.33 ± 2.57 μM, respectively.

Conclusion: According to the results obtained, the molecules used in the study may be considered potential inhibitor candidates for AChE, BChE and α-glycosidase.

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