Key residues involved in the interaction between chlorpyrifos and a chemosensory protein in Rhopalosiphum padi: Implication for tracking chemical residues via insect olfactory proteins.

The development of advanced biosensors for tracking chemical residues and detecting environmental pollution is of great significance. Insect chemical sensory proteins, including chemosensory proteins (CSPs), are easy to synthesize and purify and have been used to design proteins for specific biosensor applications. Chlorpyrifos is one of the most commonly used chemicals for controlling insect pests in agriculture. This organophosphate is harmful to aquatic species and has long-term negative consequences for the ecosystem. CSPs can bind and carry a variety of environmental chemicals, including insecticides. However, the mechanism by which CSPs bind to insecticides in aphids has not been clarified. In this study, we discovered that RpCSP1 from Rhopalosiphum padi has a higher affinity for chlorpyrifos, with a K _i value of 4.763 ± 0.491 μM. Multispectral analysis revealed the physicochemical binding mechanism between RpCSP1 and chlorpyrifos. Computational simulation analysis demonstrated that the main factor promoting the development of the RpCSP1-chlorpyrifos complex is polar solvation energy. Four residues (Arg33, Glu94, Gln145, Lys153) were essential in facilitating the interaction between RpCSP1 and chlorpyrifos. Our research has improved knowledge of the relationship between CSPs and organophosphorus pesticides. This knowledge contributes to the advancement of biosensor chips for tracking chemical residues and detecting environmental pollution through the use of CSPs.
Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
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