Therapeutic Role of Different Enzymes and Inhibitors in Alzheimer’s Disease Management

A special issue of Pharmaceuticals (ISSN 1424-8247). This special issue belongs to the section "Pharmacology".

Deadline for manuscript submissions: closed (15 December 2022) | Viewed by 2509

Special Issue Editor


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Guest Editor
Department of Medical Biotechnology, Yeungnam University, Gyeongsan 38541, Korea
Interests: Alzheimer’s disease; acetylcholinesterase inhibitors; drug discovery; natural product inhibitors; molecular docking; molecular dynamics simulation

Special Issue Information

Dear Colleagues,

Alzheimer’s disease (AD) is a predominant neurodegenerative disorder and the principal cause of dementia, affecting a large population worldwide. AD is characterized by the loss of memory and learning ability in the elderly population. Therefore, it is fundamental to seek new strategies for AD therapy for the adult population. In this regard, natural and synthetic compounds and peptides are being currently used as therapeutic agents. The different target enzymes, such as acetylcholinesterase (AChE), butyrylcholinesterase (BuChE), monoamine oxidases (MAO), β-secretase, and γ-secretase, are the key enzymes responsible for the development of AD. The development of different strategies targeting these enzymes for the management of AD would be beneficial for the elderly population. Currently, natural compounds are being utilized extensively with no or minimum toxicity against these targets for the effective management of AD.

This Special Issue aims to provide an overview of recent studies focused on innovative approaches to treat AD by targeting these enzymes with the help of molecules and drugs as candidates for developing anti-AD drugs.

Original papers, short communications, and review articles in this Special Issue may cover multidisciplinary aspects related to in silico, in vitro, and in vivo experiments.

Dr. Syed Sayeed Ahmad
Guest Editor

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Keywords

  • neurodegenerative disorder
  • alzheimer’s disease
  • acetylcholinesterase
  • butyrylcholinesterase
  • monoamine oxidases
  • β-secretase
  • γ-secretase
  • synthetic inhibitors
  • natural product inhibitors
  • drug discovery
  • molecular docking
  • molecular dynamics simulation
  • structure–activity relationships
  • molecular modeling
  • biological activity
  • enzyme kinetics

Published Papers (1 paper)

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Research

17 pages, 6547 KiB  
Article
Design, Synthesis, In Silico Testing, and In Vitro Evaluation of Thiazolidinone-Based Benzothiazole Derivatives as Inhibitors of α-Amylase and α-Glucosidase
by Shoaib Khan, Shahid Iqbal, Marwa Khan, Wajid Rehman, Mazloom Shah, Rafaqat Hussain, Liaqat Rasheed, Yousaf Khan, Ayed A. Dera, Rami Adel Pashameah, Eman Alzahrani and Abd-ElAziem Farouk
Pharmaceuticals 2022, 15(10), 1164; https://doi.org/10.3390/ph15101164 - 20 Sep 2022
Cited by 24 | Viewed by 2095
Abstract
In this study, a stepwise reaction afforded thiazolidinone-based benzothiazole derivatives 115, and the synthesized derivatives were then screened for biological significance and found to be the leading candidates against α-amylase and α-glucosidase enzymes. Almost all derivatives showed excellent to good [...] Read more.
In this study, a stepwise reaction afforded thiazolidinone-based benzothiazole derivatives 115, and the synthesized derivatives were then screened for biological significance and found to be the leading candidates against α-amylase and α-glucosidase enzymes. Almost all derivatives showed excellent to good activity ranging against α-amylase, IC50 = 2.10 ± 0.70 to 37.50 ± 0.70 μM, and α-glucosidase, IC50 = 3.20 ± 0.05 to 39.40 ± 0.80 μM. Some analogues such as 4 (2.40 ± 0.70 and 3.50 ± 0.70 μM), 5 (2.30 ± 0.05 and 4.80 ± 0.10 μM), and 6 (2.10 ± 0.70 and 3.20 ± 0.70 μM) were found with folds better activity than that of the standard drug acarbose (9.10 ± 0.10 and 10.70 ± 0.10 μM), respectively. Moreover, the structure–activity relationship (SAR) has been established for all compounds. A molecular docking study has been carried out to explore the binding interactions against α-amylase and α-glucosidase enzymes. Full article
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