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Content archived on 2024-06-18
The ß-scorpion toxin binding site as a potential target for new insecticides

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Toxin production for insecticides

Scorpion and spider toxins are difficult to produce in a laboratory or industrial setting. EU-funded researchers successfully overcame this limitation with a novel expression method in bacteria.

The project 'The ß-scorpion toxin binding site as a potential target for new insecticides' (β-TOXIN INSECTICIDE) investigated the effect of selected chemicals on mammals and insects. Researchers used techniques like patch-clamp electrophysiology to assess their effect on the voltage-gated sodium channel in the heart. A significant breakthrough was the development of an expression system for scorpion toxins in bacteria after resolving issues with protein aggregation and misfolding. This could be adapted to produce other difficult-to-produce toxins and facilitate further research on toxins. Bisphenol A (BPA) is a well-characterised plastic additive that is an environmental pollutant and endocrine disruptor. To assess the effects of BPA exposure, project members studied its interaction with the sodium channel of the heart. Results revealed that BPA blocks the current flowing through the channel but at levels far below the critical level. Through mutagenesis and via 3D molecular modelling and simulations, it was found that the BPA binding site in the channel overlaps with the local anaesthetic receptor site. Discovery of the BPA access pathway could help in designing better drugs for treating pain, heart and muscle diseases. Also study outcomes will help provide guidelines to policymakers on safe BPA exposure limits. Pyrethroids are organic chemicals that are widely used in insecticides. Through in silico modelling and ligand binding studies, project members investigated the effect of different pyrethroids on ticks and mites. Study outcomes revealed that even a single difference in amino acid can affect pyrethroid binding in sodium channels. Pyrethroids can fit into the spacious binding site of tick or mite channels unlike the physically-constricted binding site of insects. Such structural insights could help in the development of insecticides that target only selected insect species such as Varroa destructor mites. Applications include pest control, agriculture and bee cultivation. Ability to produce animal toxins insidebacteria should facilitate further research on structure-function studies and elucidate their molecular mechanisms of action. Production of designer compounds such as toxins, anaesthetics and channel blockers should enhance global food security and biomedical research.

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