Novel tribenzylaminobenzolsulphonylimine based on their pyrazine and pyridazines: Synthesis, characterization, antidiabetic, anticancer, anticholinergic, and molecular docking studies
[Display omitted] •A serie of novel tribenzylaminobenzolsulphonylimine based on their pyrazine and pyridazines was synthesised.•These precursors have been characterized by 1H and 13C NMR and FTIR spectroscopies.•Molecular docking studies of these compounds were studied.•Their inhibition effects on A...
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Published in | Bioorganic chemistry Vol. 93; p. 103313 |
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Main Authors | , , , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
SAN DIEGO
Elsevier Inc
01.12.2019
Elsevier |
Subjects | |
Online Access | Get full text |
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Summary: | [Display omitted]
•A serie of novel tribenzylaminobenzolsulphonylimine based on their pyrazine and pyridazines was synthesised.•These precursors have been characterized by 1H and 13C NMR and FTIR spectroscopies.•Molecular docking studies of these compounds were studied.•Their inhibition effects on AChE, α-glycosidase, and BChE enzymes were determined.
A new method of obtaining multifunctional pyrazoles by the reaction of 1,3-dipolar addition of tribenzylsulfonyliminochloride to polarophiles has been developed. This imine is obtained by reacting tribenzylamine with N-chlorobenzene sulfamide (chloramine-B). Regardless of the structure and composition of polarophiles, the cyclization reaction takes place in the presence of alkali in 6–8 h of boiling, which proves the activation of the methylene groups of tribenzylamine using the electron-withdrawing sulfonamide group. These novel derivatives were effective inhibitors of the α-glycosidase, butyrylcholinesterase (BChE), and acetylcholinesterase enzymes (AChE) with Ki values in the range of 0.45 ± 0.08–1.24 ± 0.27 µM for α-glycosidase, 6.04 ± 0.95–11.61 ± 2.84 µM for BChE, and 2.04 ± 0.24–4.23 ± 1.02 µM for AChE, respectively. The biological activities of the studied molecules against enzyme molecules were investigated by molecular docking calculations. The enzymes studied were AChE for ID 4M0E, BChE for ID 5NN0 BChE, and α-Glycosidase for ID 1XSI (α-Gly) respectively. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0045-2068 1090-2120 |
DOI: | 10.1016/j.bioorg.2019.103313 |