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

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.

Automated summary

An anion-mediated preorganization approach was used to design and synthesize a benzimidazolium-based calix compound R1.2 ClO4-, which was able to encapsulate DMF molecules. A nanoreactor was fabricated by using R1.2 ClO4- and l-histidine as components, showing detoxification ability for paraoxon within 30 minutes, with l-His playing a vital role in the process. The nanoreactor inhibited AChE activity, as determined by Ellman's reagent.