Thermodynamic compatibility and conformational adaptability enable the matrix-adaptive protection of glycated pea protein isolate-curcumin nanoparticles in frying oils.
The solvent effects exerted by continuous lipid matrices on nanocarrier antioxidant efficacy remain insufficiently defined. Herein, glycated pea protein isolate-curcumin nanoparticles (gPPI-CUR NPs) were engineered to elucidate their matrix-adaptive kinetic responses across frying oils with distinct saturation profiles. Protective efficacy correlated positively with lipid unsaturation, demonstrating 55.1% relative peroxide inhibition in highly unsaturated soybean oil versus 31.7% in saturated palm oil. Concurrently, the system suppressed cytotoxic aldehydes accumulation, mitigated viscosity increments, and inhibited thermal cis-to-trans isomerization. Molecular dynamics simulations elucidated this structural adaptability. The protein shell underwent conformational expansion driven by thermodynamic compatibility with linoleic acid, while the internal core maintained hydrophobic retention for ligand stability. This structural equilibrium maximized solvent-accessible surface area, increasing interfacial collision probability for in situ lipid radical scavenging. These findings generalize the dynamic balance between interfacial flexibility and core retention as a fundamental design principle for targeted lipid protection in high-stress processing.