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Paraoxonase Mimic by a Nanoreactor Aggregate Containing Benzimidazolium Calix and l ‐Histidine: Demonstration of the Acetylcholine Esterase Activity
Author(s) -
Singh Amanpreet,
Saini Sanjeev,
Kaur Navneet,
Singh Ajnesh,
Singh Narinder,
Jang Doo Ok
Publication year - 2021
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.202004944
Subject(s) - nanoreactor , chemistry , histidine , paraoxonase , dimethylformamide , paraoxon , acetylcholinesterase , enzyme , combinatorial chemistry , polymer chemistry , organic chemistry , catalysis , solvent
An anion‐mediated preorganization approach was used to design and synthesize the benzimidazolium‐based calix compound R1⋅ 2 ClO 4 − . X‐ray crystallography analysis revealed that the hydrogen‐bonding interactions between the benzimidazolium cations and N , N ‐dimethylformamide (DMF) helped R1⋅ 2 ClO 4 − encapsulate DMF molecule(s). A nanoreactor, with R1⋅ 2 ClO 4 − and l ‐histidine ( l ‐His) as the components, was fabricated by using a neutralization method. The nanoreactor could detoxify paraoxon in 30 min. l ‐His played a vital role in this process. Paraoxonase is a well‐known enzyme used for pesticide degradation. The Ellman's reagent was used to determine the percentage inhibition of the acetylcholinesterase (AChE) activity in the presence of the nanoreactor. The results indicated that the nanoreactor inhibited AChE inhibition.