Synthesis, in vitro acetylcholinesterase, butyrylcholinesterase activities and in silico molecular docking study of thiazole-thiourea hybrid derivatives

• Published in: Chemical Data Collections Vol. 45; p. 101025
• Main Authors: Ullah, Hayat, Rahim, Fazal, Taha, Muhammad, Khan, Fahad, Mehran, Alotaibi, Bader S., Zulfat, Maryam, Wadood, Abdul
• Format: Journal Article
• Language: English
• Published: Elsevier B.V 01.06.2023
• Subjects: Acetylcholinesterase; Butyrylcholinesterase; Molecular Docking; Synthesis; Thiazole; Thiourea; Thiourea; Synthesis; Acetylcholinesterase; Butyrylcholinesterase; Thiazole; Molecular Docking
• ISSN: 2405-8300; 2405-8300
• DOI: 10.1016/j.cdc.2023.101025

We have synthesized twelve thiazole-thiourea hybrid derivatives (1-12) and evaluated against acetylcholinesterase and butyrylcholinesterase enzymes. All analogues showed outstanding activities having IC50 values ranged from 0.30 ± 0.05 to 15.40 ± 0.30 µM (AChE) and 0.40 ± 0.05 to 22.70 ± 0.40 µM (BuChE) as compared to standard drug Donepezil (IC50= 2.16 ± 0.12 & 4.5 ± 0.11 µM respectively). In both cases, analogues 11 (IC50 = 0.30 ± 0.05 & 0.40 ± 0.05 µM) and analogue 12 (IC50 = 0.80 ± 0.05 & 1.10 ± 0.05 µM) withstand first and second most potent among the whole series. Structure activity relationship was carried out for all analogues which mainly depend upon number, nature, position and electron donating/withdrawing effects of the substituent/s on phenyl ring. Molecular docking study was carried out to show the binding interaction of the most potent analogue with the active site of enzyme.