Influence of colla corii asini peptides on zein nanoparticle delivery of Myricetin: structure, function and antioxidant and α‐glucosidase inhibition properties

Abstract BACKGROUND The limited water solubility and instability of myricetin (Myr) restrict its application in functional food. Peptides from colla corii asini (CCAP) have recognized potential for the design of hybrid nanoparticles due to their therapeutic bioactivity. In this study, a dual‐protein (animal–plant hybrid) delivery system was developed by the integration of CCAP with Zein (Z), with the objective of enhancing the efficiency of Myr for diabetes management. RESULTS Size‐exclusion chromatography combined with multi‐angle light scattering and zeta potential revealed small‐ and medium‐sized CCAP fragments (83.0–100.5 and 100.5–785.6 Da, 10.0% and 80.0%, respectively; degree of hydrolysis: 78.3%) enabling electrostatic interactions with Z. CCAP‐Z‐Myr nanoparticles (98.2 nm) exhibited enhanced encapsulation efficiency (91.4%) and thermal stability (endothermic peak shift from 71.8 °C (Z‐Myr) to 138 °C (CCAP‐Z‐Myr)). Fourier transform infrared spectroscopy and X‐ray diffraction confirmed Myr amorphization (disappearance of crystalline peaks at 5.8°, 11.4°, 14.1°, 16.6°, 26.3° and 28.4°) and electrostatic interactions between CCAP and Z (CO peak shift from 1657 cm −1 (Z) to 1633 cm −1 (CCAP‐Z), amide II from 1542 cm −1 (Z) to 1536 cm −1 (CCAP‐Z)). Antioxidant activity of CCAP‐Z‐Myr surpassed that of Z‐Myr (ABTS: 60.4% versus 25.3%, DPPH: 57.6% versus 33.0%, FRAP: 0.65 versus 0.42, hydroxyl radicals: 50.4% versus 30.2%, superoxide anions: 50.9% versus 29.7%). α ‐Glucosidase inhibitory activity of CCAP‐Z‐Myr was notably improved compared with Z‐Myr (78.5% versus 64.8%). CONCLUSION This study demonstrated a dual animal–plant protein strategy to enhance hydrophobic bioactive Myr delivery for diabetes management, offering novel insights for functional foods and therapeutic formulations. © 2025 Society of Chemical Industry.