Coumarin bearing triazole hybrids as cholinesterase inhibitors targeting Alzheimer's disease
Abstract
= 4.37 ± 0.91 µM for BChE and 7.17 ± 0.42 µM for AChE. Docking studies demonstrated strong binding interactions of 12c with critical residues in the active site of the enzyme. Molecular dynamics simulations confirmed the stability of the 12c-AChE and 12c-BChE complexes over 100 ns, with low RMSD values and stable hydrogen bonding. These findings highlight the importance of electronic and steric effects in optimizing cholinesterase inhibition and provide insights into the design of effective agents for Alzheimer's disease therapy.
Fields of Study & Subjects
Cholinesterase and Neurodegenerative Diseases
Synthesis and biological activity
Enzyme function and inhibition
Publication details
- Journal / source
- RSC Advances
- Publisher
- Royal Society of Chemistry (RSC)
- Volume
- 16
- Issue
- 22
- Pages
- 20364–20380
- Publication date
- 1 January 2026
- Language
- EN