Alzahrani, Abdullah Yahya AbdullahUllah, HayatRahim, FazalKhan, FahadWadood, AbdulTaha, MuhammadAl-Bagawi, AmalFareid, MohamedOthman, Mohamed S2024-03-142024-03-142024-02https://doi.org/10.1016/j.molstruc.2024.137884http://repository.msa.edu.eg/xmlui/handle/123456789/5887A series of hydroxy‑quinoline-based sulfonohydrazide derivatives (1–16) were synthesized and their structures were elucidated by using various spectroscopic tools including 1 HNMR, 13CNMR and HREI-MS and evaluated against acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE) enzymes. All synthesized derivatives showed the varied range of AChE and BuChE activities having IC50 values ranging from 0.20 ± 0.01 to 11.60 ± 0.20 µM (against AChE) and 0.80 ± 0.05 to 22.70 ± 0.30 µM (against BuChE) as compared to standard drug Donepezil (IC50 = 2.16 ± 0.12 µM & 4.5 ± 0.11 µM, respectively). Among the series, compounds 1, 8, and 10 were identified to be most potent, even more, active than standard drug having IC50 values of 0.40 ± 0.05, 0.20 ± 0.01, 0.70 ± 0.05 µM (against AChE) and 0.80 ± 0.05, 0.80 ± 0.05, 2.10 ± 0.10 µM (against BuChE) respectively. Based on the substitution pattern around the aryl ring, structure-activity relationship (SAR) analysis was conducted for all synthesized derivatives. Additionally, the molecular docking method was created to investigate the mechanism of interactions between the scaffolds that are most active and the active sites of specific AChE and BuChE enzymes.enAcetylcholinesterase; Butyrylcholinesterase and molecular docking; Hydroxy-quinoline; SulfonohydrazideArticlehttps://doi.org/10.1016/j.molstruc.2024.137884