Unveiling new thiazole-clubbed piperazine derivatives as multitarget anti-AD: Design, synthesis, and in silico studies

Arch Pharm (Weinheim). 2024 Sep;357(9):e2400044. doi: 10.1002/ardp.202400044. Epub 2024 May 16.

Abstract

New thiazole-clubbed piperazine derivatives were designed, synthesized, evaluated for their inhibitory capabilities against human acetylcholinesterase and butyrylcholinesterase (hAChE and/or hBuChE) and β-amyloid (Aβ) aggregation, and investigated for their metal chelating potential as multitarget agents for the treatment of Alzheimer's disease. Compounds 10, 19-21, and 24 showed the highest hAChE inhibitory activity at submicromolar concentrations, of which compound 10 was the most potent with a half-maximal inhibitory concentration (IC50) value of 0.151 μM. Compounds 10 and 20 showed the best hBuChE inhibitory activities (IC50 values of 0.135 and 0.103 μM, respectively), in addition to remarkable Aβ1-42 aggregation inhibitory activities and metal chelating capabilities. Both compounds were further evaluated against human neuroblastoma SH-SY5Y and PC12 neuronal cells, where they proved noncytotoxic at their active concentrations against hAChE or hBuChE. They also offered a significant neuroprotective effect against Aβ25-35-induced cytotoxicity in human neuroblastoma SH-SY5Y cells. Compound 10 displayed acceptable physicochemical properties and could pass the blood-brain barrier. The molecular docking study revealed the good binding interactions of compound 10 with the key amino acids of both the catalytic active site and the peripheral anionic site of hAChE, explaining its significant potency.

Keywords: AD; Aβ; hAChE; piperazine; thiazole.

MeSH terms

  • Acetylcholinesterase* / metabolism
  • Alzheimer Disease* / drug therapy
  • Amyloid beta-Peptides* / antagonists & inhibitors
  • Amyloid beta-Peptides* / metabolism
  • Animals
  • Butyrylcholinesterase / metabolism
  • Cell Line, Tumor
  • Cholinesterase Inhibitors* / chemical synthesis
  • Cholinesterase Inhibitors* / chemistry
  • Cholinesterase Inhibitors* / pharmacology
  • Computer Simulation
  • Dose-Response Relationship, Drug
  • Drug Design*
  • Humans
  • Molecular Docking Simulation*
  • Molecular Structure
  • Neuroprotective Agents / chemical synthesis
  • Neuroprotective Agents / chemistry
  • Neuroprotective Agents / pharmacology
  • PC12 Cells
  • Peptide Fragments / antagonists & inhibitors
  • Peptide Fragments / pharmacology
  • Piperazines* / chemical synthesis
  • Piperazines* / chemistry
  • Piperazines* / pharmacology
  • Rats
  • Structure-Activity Relationship
  • Thiazoles* / chemical synthesis
  • Thiazoles* / chemistry
  • Thiazoles* / pharmacology

Substances

  • Cholinesterase Inhibitors
  • Thiazoles
  • Piperazines
  • Amyloid beta-Peptides
  • Acetylcholinesterase
  • Neuroprotective Agents
  • Butyrylcholinesterase
  • Peptide Fragments
  • amyloid beta-protein (1-42)

Grants and funding