Protein-based multidimensional stabilization of nanopesticides

Nanopesticides offer new avenues to reduce pesticide application, improve efficacy, and enable precise delivery, but their field translation is constrained by stability across storage, dilution, spraying, environmental exposure, and target deposition. They are susceptible to aggregation, Ostwald ripening, coalescence, photodegradation, thermal/hydrolytic degradation, poor foliar retention, wash-off, and premature release. Conventional surfactant-, polymer-, or inorganic particle-based strategies are limited by mono-functional mechanisms and poor adaptability to coupled multifactorial stresses. As natural amphiphilic macromolecules, proteins possess interfacial adsorption, self-assembly, environmental responsiveness, and biocompatibility. Through synergistic hydrogen bonding, electrostatic interactions, hydrophobic forces, and disulfide reorganization, proteins form adaptive networks that provide five stability dimensions: colloidal stability via steric/electrostatic repulsion; interfacial film stability via dense adsorption layers inhibiting coalescence; environmental stability via protective matrices against UV, thermal, and pH stresses; foliar retention stability via amyloid-like in situ films enhancing adhesion and rainfastness; and functional release stability via stimuli-responsive disassembly and enzyme-triggered degradation. This review summarizes the molecular basis, mechanisms, and advances of protein-mediated stabilization, and further discusses the sustainability, biodegradability, biocompatibility, and environmental safety considerations that will govern its translation toward next-generation sustainable nanopesticide formulations.