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Amyloid‐Like Protein Aggregation Toward Pesticide Reduction
Pesticide overuse is a major global problem and the cause of this problem is noticeable pesticide loss from undesired bouncing of sprayed pesticide droplets and rain erosion. This further becomes a primary source of soil and groundwater pollution. Herein, the authors report a method that can enhance...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9069373/ https://www.ncbi.nlm.nih.gov/pubmed/35257513 http://dx.doi.org/10.1002/advs.202105106 |
Sumario: | Pesticide overuse is a major global problem and the cause of this problem is noticeable pesticide loss from undesired bouncing of sprayed pesticide droplets and rain erosion. This further becomes a primary source of soil and groundwater pollution. Herein, the authors report a method that can enhance pesticide droplet deposition and adhesion on superhydrophobic plant leave surfaces by amyloid‐like aggregation of bovine serum albumin (BSA). Through the reduction of the disulfide bond of BSA by tris(2‐carboxyethyl) phosphine hydrochloride (TCEP), the amyloid‐like phase transition of BSA is triggered that rapidly affords abundant phase‐transitioned BSA (PTB) oligomers to facilitate the invasion of the PTB droplet into the nanostructures on a leaf surface. Such easy penetration is further followed by a robust amyloid‐mediated interfacial adhesion of PTB on leaf surface. As a result, after mixing with pesticides, the PTB system exhibits a remarkable pesticide adhesion capacity that is more than 10 times higher than conventional fixation of commercial pesticides. The practical farmland experiments show that the use of PTB aggregation could reduce the use of pesticides by 70–90% while ensuring yield. This work demonstrates that current pesticide dosage in actual agriculture production may be largely reduced by utilizing eco‐friendly amyloid‐like protein aggregation. |
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