Synthesis and biological evaluation of substituted benzohydrazide Schiff base adduct as potential cholinesterase inhibitors

• Published in: CHEMICAL DATA COLLECTIONS
• Main Authors: Zulfiqar, Ahmad; Khan, Irshad Ullah; Nabi, Muhammad; Ullah, Hayat; Iqbal, Naveed; Zeb, Benish; Hussain, Amjad; Khan, Daud; Rab, Abdur; Junaid, Sayyed Muhammad; Taha, Muhammad; Shah, Syed Adnan Ali; Rahim, Fazal
• Format: Article
• Language: English
• Published: ELSEVIER 2024
• Subjects: Chemistry
• Online Access: https://www-webofscience-com.uitm.idm.oclc.org/wos/woscc/full-record/WOS:001333598600001
• ISSN: 2405-8300
• DOI: 10.1016/j.cdc.2024.101151

A total of Twenty two (22) 22 ) derivatives of benzohydrazide bearing Schiff base have been synthesized, characterized through 1 HNMR, 13 C NMR and screened against cholinesterase inhibitory potentials. All the adducts ( 1-22 ) showed varying degree of cholinesterase inhibitory potential IC50 50 ranging between 13.23 f 0.02 to 59.09 f 1.22 mu M against acetylcholinesterase, with IC50 50 values ranging from 23.55 f 0.32 to 61.55 f 0.58 mu M against butyrylcholinesterase. Among the series analogs 1, 3, 8, 12, 14, 15, 17, 18 and 22 with IC50 50 values 20.05 f 0.13, 17.32 f 0.15, 14.32 f 0.97, 23.33 f 0.56, 18.02 f 0.09, 19.05 f 0.13, 15.11 f 0.23, 13.23 f 0.02, and 22.57 f 0.09 mu M respectively showed excellent inhibitory potential against acetylcholinesterase and with IC50 50 values 31.46 f 0.98, 26.06 f 0.08, 25.33 f 1.49, 30.12 f 0.78, 28.11 f 0.5, 29.33 f 0.19, 25.37 f 0.47, 23.55 f 0.32 and 33.12 f 0.78 against butylcholinesterase as compared to the standard Galanthamine. All other analogs showed moderate inhibitory potential. A structure- activity relationship has been established for all compounds. Through molecular docking studies, the interactions between compounds with the enzyme active sites were confirmed.