Cholinesterases Inhibition by Novel cis- and trans-3-Arylaminocyclohexyl N,N-Dimethylcarbamates: Biological Evaluation and Molecular Modeling
AUTOR(ES)
Yamazaki, Diego A. S., Cândido, Augusto A., Bagatin, Mariane C., Machinski Jr., Miguel, Mossini,, Simone A. G., Pontes, Rodrigo M., Rosa, Fernanda A., Basso, Ernani A., Gauze, Gisele F.
FONTE
J. Braz. Chem. Soc.
DATA DE PUBLICAÇÃO
2016-09
RESUMO
The present study describes the synthesis, assessment of the anticholinesterase activity and the inhibition type of novel cis- and trans-3-arylaminocyclohexyl N,N-dimethylcarbamates. In vitro inhibition assay by Ellman's method with human blood samples showed that carbamates were selective for butyrylcholinesterase (BuChE) with compound concentration that inhibits 50% of enzyme activity (IC50) between 0.11 and 0.18 mmol L-1. cis- and trans-3-(4-Methoxyphenylamino)cyclohexyl N,N-dimethylcarbamate hydrochloride were the most active for BuChE, showing that the presence of methoxyl group enhanced the anticholinesterase activity. The enzyme kinetics studies indicate a noncompetitive inhibition against acetylcholinesterase (AChE) and mixed type inhibition for BuChE. Molecular modeling studies confirm the ability of carbamates to bind both the active and peripheral sites of the BuChE.
Documentos Relacionados
- Molecular modeling and anticholinesterasic activity of novel 2-arylaminocyclohexyl N,N-dimethylcarbamates
- Novel Actinomycins Formed by Biosynthetic Incorporation of cis- and trans-4-Methylproline
- cis- and trans-acting regulatory elements of the yeast URA3 promoter.
- cis- and trans-Acting Elements in Flavivirus RNA Replication†
- Repair synthesis by human cell extracts in DNA damaged by cis- and trans-diamminedichloroplatinum(II).
