Physico-Chemical Study on the Mechanism of Interaction Between Divalent and Trivalent Iron Double Oxide Nanoparticles With Fibrillar Protein-Gelatin

Abstract

The study investigates the interaction mechanism between ferrum(II, III) oxide (Fe₃O₄) nanoparticles and the fibrillar protein gelatin (Gel) using a set of physicochemical methods. For the first time, it was established that the formation of a stable intermolecular complex is due to the amphiphilic and clusterophilic properties of Fe₃O₄ nanoparticles, their ability to polarize, electrostatic interactions, and the formation of supramolecular structures. Absorption in the region of 260 nm (UV-Vis spectroscopy) indicates the formation of plasmon resonance in the NPFe₃O₄/Gel system. Dynamic Light Scattering (DLS) revealed an average hydrodynamic particle diameter of approximately 79.0 nm, which is consistent with X-ray diffraction (XRD) data and confirms the chemisorption of the Gel protein on the surface of Fe₃O₄ nanoparticles. The work has scientific novelty in understanding the specifics of biopolymer binding with metal oxide nanostructures.