1, 3‐dipolar cycloaddition reactions of the compound obtaining from cyclopentadiene‐PTAD and biological activities of adducts formed selectively. (27th December 2021)

• Record Type: Journal Article
• Authors: Yavari, Mirali Akbar; Taslimi, Parham; Bayrak, Cetin; Taskin‐Tok, Tugba; Menzek, Abdullah
• Is Part Of: Journal of heterocyclic chemistry. Volume 59:Number 5(2022)
• Page Start: 864
• Page End: 878
• Publication Date: 2021-12-27
• Subjects: Heterocyclic compounds -- Periodicals; 547.59
• DOI: 10.1002/jhet.4426
• Languages: English
• ISSNs: 0022-152X

Abstract

Abstract: After known adduct (4 ) was synthesized by cycloaddition reaction of cyclopentadiene with 4‐phenyl‐1, 2, 4‐triazoline‐3, 5‐dione, seven new isoxazoline derivatives were synthesized from reactions of 4 with corresponding oximes prepared from benzaldehyde derivatives in the existence of the aqueous NaOCl in CH2 Cl2 at 0°C—RT via nitrile oxides. Four new pyrazoline derivatives were also synthesized from reactions of 4 with corresponding prepared reagents via nitrile imines. Selectively, each of all isoxazole and pyrazoline derivatives was synthesized by 1, 3‐dipolar cycloaddition reactions of compound 4 with the corresponding reagents. Based on the results of their biological activity analyses, K i values for acetylcholinesterase (AChE), butyrylcholinesterase (BChE), and alpha‐glucosidase (α‐Gly) enzymes were obtained in this range 32.15 ± 5.73–107.44 ± 19.52 22.57 ± 4.30–186.07 ± 23.51, and 69.08 ± 8.54–528.07 ± 38.46 nM, respectively. Besides that, these compounds were subjected to molecular docking to describe the interaction against AChE, BChE, and α‐Gly enzymes in which important interactions were visualized and evaluated with residues of the binding region in each target enzyme. Abstract : After known adduct (4 ) was synthesized by cycloaddition reaction of cyclopentadiene with 4‐phenyl‐1, 2, 4‐triazoline‐3, 5‐dione, new seven isoxazoline and four pyrazoline derivatives were selectively synthesized from reactions of 4 with nitrile oxides and nitrile imines. Based on the results of their biological activity analyses, Ki values for acetylcholinesterase (AChE), butyrylcholinesterase (BChE), and alpha‐glucosidase (α‐Gly) enzymes were obtained in this range 32.15 ± 5.73–107.44 ± 19.52 22.57 ± 4.30–186.07 ± 23.51, and 69.08 ± 8.54–528.07 ± 38.46 nM, respectively