Interactions between curcumin and fish−/bovine-derived (type I and II) collagens: Preparation of nanoparticle and their application in Pickering emulsions

This study aims to elucidate the interaction mechanisms between curcumin (Cur) and four collagen subtypes (fish type I [FCI], bovine type I [BCI], fish type II [FCII], bovine type II [BCII]), with parallel characterization of the structural and functional attributes of their derived nanoparticles. Type I Collagen/Cur nanoparticles exhibited superior solution stability compared to type II. Cur binding significantly enhanced the surface hydrophobicity, absolute ζ potential, and surface tension of collagen, while reduced dynamic interfacial tension. The binding type of Cur to collagen was static, and binding process was enthalpy-driven exothermic reaction. Molecular dynamics simulations revealed that hydrophobic interactions, hydrogen bonds, and electrostatic forces dominated the binding process. The binding affinity followed the order: FCI/Cur > BCI/Cur > FCII/Cur > BCII/Cur. The binding sites of Cur to type I collagen and type II collagen were around Ser129-Glu135 and Asn179-Ser183 residues. Collagen/Cur nanoparticle stabilized emulsions and improved oxidative stability and storage modulus.