Determination of chlorothalonil levels through inhibitory effect on papain activity at protein-decorated liquid crystal interfaces.

Abstract

A liquid crystal (LC)-based assay was developed to detect chlorothalonil (CHL). The detection principle is based on (i) the electrostatic interaction between the positively charged protein protamine (PRO) with the negatively charged phospholipid dioleoyl-sn-glycero-3-phospho-rac-(1-glycerol) sodium salt (DOPG) and (ii) the CHL-mediated inhibition of papain (PAP) activity. The aqueous/LC interface was decorated with a monolayer of DOPG and PRO that self-assembled via electrostatic interactions. PAP can hydrolyze PRO, resulting in the realignment of an LC by DOPG, inducing a shift in the LC response from bright to dark. The addition of CHL can inhibit the activity of PAP, leading to the attraction of PRO to DOPG and the consequent disruption of the LC orientation. The orientation change of the LC in the presence or absence of CHL can be observed from the changes in its optical appearance using a polarized light microscope. Under optimal conditions, the developed assay achieved a detection limit of 0.196 pg mL−1 within a range of determination of 0.65–200 pg mL−1. The selectivity of the assay was verified in the presence of carbendazim and imidacloprid. The practical application of the proposed assay was demonstrated by its use to determine the levels of CHL in food extracts and environmental samples, which yielded recoveries and relative standard deviations (RSD) in the ranges of 87.39–99.663% and 1.03–6.32%, respectively.Graphical abstract Supplementary InformationThe online version contains supplementary material available at 10.1007/s00604-022-05396-1.