New Materials, Compounds and Applications

This study investigates the binding affinities of compounds selected from the ZINC database to acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) enzymes using molecular docking, molecular dynamics simulations and MMGBSA calculations. The results indicate that the selected compounds exhibit strong binding to AChE, outperforming standard inhibitors such as galantamine and donepezil. Key amino acid residues contributing to the stabilization of the enzyme-inhibitor complexes were identified. The analysis highlights the critical role of van der Waals and electrostatic interactions in maintaining binding stability. The obtained results suggest that the selected compounds from the ZINC database represent promising candidates for the development of novel acetylcholinesterase inhibitors and may encourage further experimental and pharmacological investigations.