Paraoxonase Mimic by a Nanoreactor Aggregate Containing Benzimidazolium Calix and l-Histidine: Demonstration of the Acetylcholine Esterase Activity

Amanpreet Singh, Sanjeev Saini, Mayank, Navneet Kaur, Ajnesh Singh, Narinder Singh, Doo Ok Jang

Research output: Contribution to journalArticlepeer-review

Abstract

An anion-mediated preorganization approach was used to design and synthesize the benzimidazolium-based calix compound R1⋅2 ClO4. X-ray crystallography analysis revealed that the hydrogen-bonding interactions between the benzimidazolium cations and N,N-dimethylformamide (DMF) helped R1⋅2 ClO4 encapsulate DMF molecule(s). A nanoreactor, with R1⋅2 ClO4 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.

Original languageEnglish
Pages (from-to)5737-5744
Number of pages8
JournalChemistry - A European Journal
Volume27
Issue number18
DOIs
Publication statusPublished - 2021 Mar 26

Bibliographical note

Funding Information:
This work was supported by a research grant from the SERB Project (Project No. EMR/2017/003438). A.S. is thankful to IIT Ropar for the institute's postdoctoral fellowship.

Publisher Copyright:
© 2020 Wiley-VCH GmbH

All Science Journal Classification (ASJC) codes

  • Catalysis
  • Organic Chemistry

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