1. JCCT
  2. Ch&ChT Vol. 20, No. 1, 2026
  3. Physico-Chemical Study on the Mechanism of Interaction Between Divalent and Trivalent Iron Double Oxide Nanoparticles With Fibrillar Protein-Gelatin

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

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Iryna Tsykhanovska1, Tetiana Lazarieva1, Olexandr Alexandrov1, Mykola Riabchykov2, Alla Koval3, Oksana Bryzytska4
Affiliation: 
1 V.N. Karazin Kharkiv National University, 4 Svobody Sq., Kharkiv 61022, Ukraine 2 Lutsk National Technical University, 75 Lvivska St., Lutsk 43018, Ukraine 3 National University of Pharmacy, 53 H. Skovorody St., Kharkiv 61002, Ukraine 4 PIHE "Kharkiv International Medical University", 38 Molochna St., Kharkiv 61001, Ukraine oksanabrizi69@gmail.com
DOI: 
https://doi.org/
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Keywords: 
Fe₃O₄ nanoparticles
gel
chemisorption
nano аssociates
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.
References: 

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