najoNanosystems: Physics, Chemistry, MathematicsНаносистемы: физика, химия, математика2220-80542305-7971Университет ИТМОnajo-1495Research ArticleCHEMISTRY AND MATERIALS SCIENCEХИМИЯ И НАУКА О МАТЕРИАЛАХPhysicochemical Aspects and Cellular Effects of Nanoceria–Human Serum Albumin Conjugateshttps://orcid.org/0000-0002-8243-6339ProskurninaElena V.

Chief Research Scientist, 8072-7745

proskurnina@gmail.comhttps://orcid.org/0000-0002-6336-9900KostyukSvetlana V.

Head of the Laboratory, 4022-8214

svet-vk@yandex.ruhttps://orcid.org/0000-0002-5868-4746SozarukovaMadina M.

Senior Researcher, 9268-1063

s_madinam@bk.ruhttps://orcid.org/0000-0003-1206-5832ErshovaElizaveta S.

Leading Research Scientist, 5488-0201

es-ershova@rambler.ruhttps://orcid.org/0000-0003-1847-0548VeikoNatalia N.

Chief Research Scientist, 8477-2627

satelit32006@yandex.ruhttps://orcid.org/0000-0002-9811-6241PopkovMatvei A.

Junior Research

ma_popkov@igic.ras.ruhttps://orcid.org/0000-0001-7033-6843KostyukEdmund V.

Leading Research Scientist

edmundvk@ya.ruhttps://orcid.org/0000-0002-6697-8306MartynovAndrey V.

Senior Researcher, 6642-6360

avlamar@mail.ruhttps://orcid.org/0000-0003-2343-2140IvanovVladimir K.

Head of the Research Institute, 8732-4200

van@igic.ras.ruKurnakov Institute of General and Inorganic Chemistry of the Russian Academy of SciencesRussian FederationPetrovsky Russian Scientific Center of Surgery, Institute of Longevity with a Clinic of Rehabilitation and Preventive MedicineRussian Federation2025050220261651495Copyright © Proskurnina E.V., Kostyuk S.V., Sozarukova M.M., Ershova E.S., Veiko N.N., Popkov M.A., Kostyuk E.V., Martynov A.V., Ivanov V.K., 20252025Proskurnina E.V., Kostyuk S.V., Sozarukova M.M., Ershova E.S., Veiko N.N., Popkov M.A., Kostyuk E.V., Martynov A.V., Ivanov V.K.Proskurnina E.V., Kostyuk S.V., Sozarukova M.M., Ershova E.S., Veiko N.N., Popkov M.A., Kostyuk E.V., Martynov A.V., Ivanov V.K.Данная работа распространяется под лицензией Creative Commons Attribution 4.0.This work is licensed under a Creative Commons Attribution 4.0 License.https://nanojournal.ifmo.ru/jour/article/view/1495

Nanoceria exhibits unique catalytic properties towards reactive oxygen species (ROS), which act as mediators of key signaling pathways. Albumin is the most abundant blood protein, and its interaction with nanoceria modifies the properties of both nanoceria and albumin. Using an in vitro model of human embryonic lung fibroblasts, we investigated biochemical properties of nanoceria–albumin conjugates towards cell viability, intracellular reactive oxygen species, expression of NOX4, NRF2, and NF-κB, oxidative DNA damage/repair, apoptosis, cell proliferation, and autophagy. The results demonstrate that albumin binding alters the physicochemical properties of nanoceria, promoting efficient cellular uptake through modulation of surface interactions. This conjugation attenuates nanoceria’s influence on intracellular reactive oxygen species equilibrium and mitochondrial membrane potential by modifying nanoparticle-protein interfacial dynamics. Notably, albumin-bound nanoceria induces a stronger activation of NOX4, resulting in increased genotoxic stress; however, the enhanced activation of DNA repair pathways mitigates this damage more efficiently than bare nanoceria. Furthermore, albumin-to-nanoceria conjugation modulates signaling pathways by enhancing suppression of the pro-inflammatory NF-κB cascade and stimulating autophagic processes. Overall, the physicochemical effects of nanoceria modification due to albumin conjugation reduce cytotoxicity of nanoceria while augmenting its anti-inflammatory and regenerative potential.

nanoceriahuman serum albumincytotoxicitygenotoxicityoxidative metabolism genesproliferationautophagyhuman lung embryonic fibroblaststhe Russian Science Foundation, project No. 24-13-00370ReferencesKorsvik C., Patil S., Seal S. et al. Superoxide dismutase mimetic properties exhibited by vacancy engineered ceria nanoparticles. Chem. Commun., 2007, 10, 1056.Korsvik C., Patil S., Seal S. et al. Superoxide dismutase mimetic properties exhibited by vacancy engineered ceria nanoparticles. Chem. Commun., 2007, 10, 1056.Ivanov V.K., Usatenko A.V., Shcherbakov A.B. Antioxidant activity of nanocrystalline ceria to anthocyanins. Russ. J. Inorg. Chem., 2009, 54(10), 1522–1527.Ivanov V.K., Usatenko A.V., Shcherbakov A.B. Antioxidant activity of nanocrystalline ceria to anthocyanins. Russ. J. Inorg. Chem., 2009, 54(10), 1522–1527.Pirmohamed T., Dowding J.M., Singh S. et al. Nanoceria exhibit redox state-dependent catalase mimetic activity. Chem. Commun., 2010, 46(16), 2736.Pirmohamed T., Dowding J.M., Singh S. et al. Nanoceria exhibit redox state-dependent catalase mimetic activity. Chem. Commun., 2010, 46(16), 2736.Asati A., Santra S., Kaittanis C. et al. Oxidase‐Like Activity of Polymer‐Coated Cerium Oxide Nanoparticles. Angew. Chemie Int. Ed., 2009, 48(13), 2308–2312.Asati A., Santra S., Kaittanis C. et al. Oxidase‐Like Activity of Polymer‐Coated Cerium Oxide Nanoparticles. Angew. Chemie Int. Ed., 2009, 48(13), 2308–2312.Liu B., Huang Z., Liu J. Boosting the oxidase mimicking activity of nanoceria by fluoride capping: rivaling protein enzymes and ultrasensitive F− detection. Nanoscale, 2016, 8(28), 13562–13567.Liu B., Huang Z., Liu J. Boosting the oxidase mimicking activity of nanoceria by fluoride capping: rivaling protein enzymes and ultrasensitive F− detection. Nanoscale, 2016, 8(28), 13562–13567.Yao T., Tian Z., Zhang Y. et al. Phosphatase-like Activity of Porous Nanorods of CeO2 for the Highly Stabilized Dephosphorylation under Interferences. ACS Appl. Mater. Interfaces, 2019, 11(1), 195–201.Yao T., Tian Z., Zhang Y. et al. Phosphatase-like Activity of Porous Nanorods of CeO2 for the Highly Stabilized Dephosphorylation under Interferences. ACS Appl. Mater. Interfaces, 2019, 11(1), 195–201.Tian Z., Yao T., Qu C. et al. Photolyase-Like Catalytic Behavior of CeO2. Nano Lett., 2019, 19(11), 8270–8277.Tian Z., Yao T., Qu C. et al. Photolyase-Like Catalytic Behavior of CeO2. Nano Lett., 2019, 19(11), 8270–8277.Khulbe K., Karmakar K., Ghosh S. et al. Nanoceria-Based Phospholipase-Mimetic Cell Membrane Disruptive Antibiofilm Agents. ACS Appl. Bio Mater., 2020, 3(7), 4316–4328.Khulbe K., Karmakar K., Ghosh S. et al. Nanoceria-Based Phospholipase-Mimetic Cell Membrane Disruptive Antibiofilm Agents. ACS Appl. Bio Mater., 2020, 3(7), 4316–4328.Xu F., Lu Q., Huang P.-J.J. et al. Nanoceria as a DNase I mimicking nanozyme. Chem. Commun., 2019, 55(88), 13215–13218.Xu F., Lu Q., Huang P.-J.J. et al. Nanoceria as a DNase I mimicking nanozyme. Chem. Commun., 2019, 55(88), 13215–13218.Wu N., Liu T., Tian M. et al. Albumin, an interesting and functionally diverse protein, varies from ‘native’ to ‘effective’ (Review). Mol. Med. Rep., 2023, 29(2), 24.Wu N., Liu T., Tian M. et al. Albumin, an interesting and functionally diverse protein, varies from ‘native’ to ‘effective’ (Review). Mol. Med. Rep., 2023, 29(2), 24.Tao C., Chuah Y.J., Xu C. et al. Albumin conjugates and assemblies as versatile bio-functional additives and carriers for biomedical applications. J. Mater. Chem. B, 2019, 7(3), 357–367.Tao C., Chuah Y.J., Xu C. et al. Albumin conjugates and assemblies as versatile bio-functional additives and carriers for biomedical applications. J. Mater. Chem. B, 2019, 7(3), 357–367.Qu N., Song K., Ji Y. et al. Albumin Nanoparticle-Based Drug Delivery Systems. Int. J. Nanomedicine, 2024, 19, 6945–6980.Qu N., Song K., Ji Y. et al. Albumin Nanoparticle-Based Drug Delivery Systems. Int. J. Nanomedicine, 2024, 19, 6945–6980.Tincu C.-E., Andrițoiu C.V., Popa M. et al. Recent Advancements and Strategies for Overcoming the Blood–Brain Barrier Using Albumin-Based Drug Delivery Systems to Treat Brain Cancer, with a Focus on Glioblastoma. Polymers (Basel), 2023, 15(19), 3969.Tincu C.-E., Andrițoiu C.V., Popa M. et al. Recent Advancements and Strategies for Overcoming the Blood–Brain Barrier Using Albumin-Based Drug Delivery Systems to Treat Brain Cancer, with a Focus on Glioblastoma. Polymers (Basel), 2023, 15(19), 3969.Butterfield A.D., Wang B., Wu P. et al. Plasma and Serum Proteins Bound to Nanoceria: Insights into Pathways by which Nanoceria may Exert Its Beneficial and Deleterious Effects In Vivo. J. Nanomed. Nanotechnol., 2020, 11(4), 546.Butterfield A.D., Wang B., Wu P. et al. Plasma and Serum Proteins Bound to Nanoceria: Insights into Pathways by which Nanoceria may Exert Its Beneficial and Deleterious Effects In Vivo. J. Nanomed. Nanotechnol., 2020, 11(4), 546.Fanciullino R., Ciccolini J., Milano G. Challenges, expectations and limits for nanoparticles-based therapeutics in cancer: A focus on nano-albumin-bound drugs. Crit. Rev. Oncol. Hematol., 2013, 88(3), 504–513.Fanciullino R., Ciccolini J., Milano G. Challenges, expectations and limits for nanoparticles-based therapeutics in cancer: A focus on nano-albumin-bound drugs. Crit. Rev. Oncol. Hematol., 2013, 88(3), 504–513.Zhu Y., Xue J., Chen W. et al. Albumin-biomineralized nanoparticles to synergize phototherapy and immunotherapy against melanoma. J. Control. Release, 2020, 322, 300–311.Zhu Y., Xue J., Chen W. et al. Albumin-biomineralized nanoparticles to synergize phototherapy and immunotherapy against melanoma. J. Control. Release, 2020, 322, 300–311.Gou Y., Zhang Z., Qi J. et al. Folate-functionalized human serum albumin carrier for anticancer copper(II) complexes derived from natural plumbagin. J. Inorg. Biochem., 2015, 153, 13–22.Gou Y., Zhang Z., Qi J. et al. Folate-functionalized human serum albumin carrier for anticancer copper(II) complexes derived from natural plumbagin. J. Inorg. Biochem., 2015, 153, 13–22.Kim D., Amatya R., Hwang S. et al. BSA-Silver Nanoparticles: A Potential Multimodal Therapeutics for Conventional and Photothermal Treatment of Skin Cancer. Pharmaceutics, 2021, 13(4), 575.Kim D., Amatya R., Hwang S. et al. BSA-Silver Nanoparticles: A Potential Multimodal Therapeutics for Conventional and Photothermal Treatment of Skin Cancer. Pharmaceutics, 2021, 13(4), 575.Jaiswal V.D., Pangam D.S., Dongre P.M. Biophysical study of cisplatin loaded albumin-gold nanoparticle and its interaction with glycans of gp60 receptor. Int. J. Biol. Macromol., 2023, 231, 123368.Jaiswal V.D., Pangam D.S., Dongre P.M. Biophysical study of cisplatin loaded albumin-gold nanoparticle and its interaction with glycans of gp60 receptor. Int. J. Biol. Macromol., 2023, 231, 123368.Korolev D., Shumilo M., Shulmeyster G. et al. Hemolytic Activity, Cytotoxicity, and Antimicrobial Effects of Human Albumin- and Polysorbate-80-Coated Silver Nanoparticles. Nanomaterials, 2021, 11(6), 1484.Korolev D., Shumilo M., Shulmeyster G. et al. Hemolytic Activity, Cytotoxicity, and Antimicrobial Effects of Human Albumin- and Polysorbate-80-Coated Silver Nanoparticles. Nanomaterials, 2021, 11(6), 1484.Park H.-Y., Chung C., Eiken M.K. et al. Silver nanoparticle interactions with glycated and non-glycated human serum albumin mediate toxicity. Front. Toxicol., 2023, 5, 1081753.Park H.-Y., Chung C., Eiken M.K. et al. Silver nanoparticle interactions with glycated and non-glycated human serum albumin mediate toxicity. Front. Toxicol., 2023, 5, 1081753.Chen J.L.-Y., Yang S.-J., Pan C.-K. et al. Cisplatin and Albumin-Based Gold–Cisplatin Nanoparticles Enhance Ablative Radiation Therapy–Induced Antitumor Immunity in Local and Distant Tumor Microenvironment. Int. J. Radiat. Oncol., 2023, 116(5), 1135–1149.Chen J.L.-Y., Yang S.-J., Pan C.-K. et al. Cisplatin and Albumin-Based Gold–Cisplatin Nanoparticles Enhance Ablative Radiation Therapy–Induced Antitumor Immunity in Local and Distant Tumor Microenvironment. Int. J. Radiat. Oncol., 2023, 116(5), 1135–1149.Gou Y., Zhang Y., Qi J. et al. Enhancing the copper(II) complexes cytotoxicity to cancer cells through bound to human serum albumin. J. Inorg. Biochem., 2015, 144 47–55.Gou Y., Zhang Y., Qi J. et al. Enhancing the copper(II) complexes cytotoxicity to cancer cells through bound to human serum albumin. J. Inorg. Biochem., 2015, 144 47–55.He C., Xie M., Hong F. et al. A Highly Sensitive Glucose Biosensor Based on Gold Nanoparticles/Bovine Serum Albumin/Fe3O4 Biocomposite Nanoparticles. Electrochim. Acta, 2016, 222, 1709–1715.He C., Xie M., Hong F. et al. A Highly Sensitive Glucose Biosensor Based on Gold Nanoparticles/Bovine Serum Albumin/Fe3O4 Biocomposite Nanoparticles. Electrochim. Acta, 2016, 222, 1709–1715.Janani B., Raju L.L., Thomas A.M. et al. Impact of bovine serum albumin – A protein corona on toxicity of ZnO NPs in environmental model systems of plant, bacteria, algae and crustaceans. Chemosphere, 2021, 270, 128629.Janani B., Raju L.L., Thomas A.M. et al. Impact of bovine serum albumin – A protein corona on toxicity of ZnO NPs in environmental model systems of plant, bacteria, algae and crustaceans. Chemosphere, 2021, 270, 128629.Bhushan B., Gopinath P. Antioxidant nanozyme: a facile synthesis and evaluation of the reactive oxygen species scavenging potential of nanoceria encapsulated albumin nanoparticles. J. Mater. Chem. B, 2015, 3(24), 4843–4852.Bhushan B., Gopinath P. Antioxidant nanozyme: a facile synthesis and evaluation of the reactive oxygen species scavenging potential of nanoceria encapsulated albumin nanoparticles. J. Mater. Chem. B, 2015, 3(24), 4843–4852.Yang Z., Luo S., Zeng Y. et al. Albumin-Mediated Biomineralization of Shape-Controllable and Biocompatible Ceria Nanomaterials. ACS Appl. Mater. Interfaces, 2017, 9(8), 6839–6848.Yang Z., Luo S., Zeng Y. et al. Albumin-Mediated Biomineralization of Shape-Controllable and Biocompatible Ceria Nanomaterials. ACS Appl. Mater. Interfaces, 2017, 9(8), 6839–6848.Yeni Y., Genc S., Nadaroglu H. et al. Effects of quercetin-immobilized albumin cerium oxide nanoparticles on glutamate toxicity: in vitro study. Naunyn. Schmiedebergs. Arch. Pharmacol., 2025, 398 (5), 5147–5156.Yeni Y., Genc S., Nadaroglu H. et al. Effects of quercetin-immobilized albumin cerium oxide nanoparticles on glutamate toxicity: in vitro study. Naunyn. Schmiedebergs. Arch. Pharmacol., 2025, 398 (5), 5147–5156.Khoshgozaran Roudbaneh S.Z., Kahbasi S., Sohrabi M.J. et al. Albumin binding, antioxidant and antibacterial effects of cerium oxide nanoparticles. J. Mol. Liq., 2019, 296, 111839.Khoshgozaran Roudbaneh S.Z., Kahbasi S., Sohrabi M.J. et al. Albumin binding, antioxidant and antibacterial effects of cerium oxide nanoparticles. J. Mol. Liq., 2019, 296, 111839.Shcherbakov A.B., Teplonogova M.A., Ivanova O.S. et al. Facile method for fabrication of surfactant-free concentrated CeO2 sols. Mater. Res. Express, 2017, 4(5), 055008.Shcherbakov A.B., Teplonogova M.A., Ivanova O.S. et al. Facile method for fabrication of surfactant-free concentrated CeO2 sols. Mater. Res. Express, 2017, 4(5), 055008.Creed S., McKenzie M. Measurement of Mitochondrial Membrane Potential with the Fluorescent Dye Tetramethylrhodamine Methyl Ester (TMRM). Methods Mol. Biol., 2019, 1928, 69–76.Creed S., McKenzie M. Measurement of Mitochondrial Membrane Potential with the Fluorescent Dye Tetramethylrhodamine Methyl Ester (TMRM). Methods Mol. Biol., 2019, 1928, 69–76.Luik A.I., Naboka Y.N., Mogilevich S.E. et al. Study of human serum albumin structure by dynamic light scattering: two types of reactions under different pH and interaction with physiologically active compounds. Spectrochim. Acta Part A Mol. Biomol. Spectrosc., 1998, 54(10), 1503–1507.Luik A.I., Naboka Y.N., Mogilevich S.E. et al. Study of human serum albumin structure by dynamic light scattering: two types of reactions under different pH and interaction with physiologically active compounds. Spectrochim. Acta Part A Mol. Biomol. Spectrosc., 1998, 54(10), 1503–1507.Velichko E., Makarov S., Nepomnyashchaya E. et al. Molecular Aggregation in Immune System Activation Studied by Dynamic Light Scattering. Biology (Basel), 2020, 9(6), 123.Velichko E., Makarov S., Nepomnyashchaya E. et al. Molecular Aggregation in Immune System Activation Studied by Dynamic Light Scattering. Biology (Basel), 2020, 9(6), 123.Bardik V., Gotsulskii V., Pavlov E. et al. Light scattering study of human serum albumin in pre-denaturation: Relation to dynamic transition in water at 42°C. J. Mol. Liq., 2012, 176, 60–64.Bardik V., Gotsulskii V., Pavlov E. et al. Light scattering study of human serum albumin in pre-denaturation: Relation to dynamic transition in water at 42°C. J. Mol. Liq., 2012, 176, 60–64.Liu Y., Yang Z., Zhang X. et al. Shape/Crystal Facet of Ceria Induced Well-Dispersed and Stable Au Nanoparticles for the Selective Hydrogenation of Phenylacetylene. Catal. Letters, 2019, 149(2), 361–372.Liu Y., Yang Z., Zhang X. et al. Shape/Crystal Facet of Ceria Induced Well-Dispersed and Stable Au Nanoparticles for the Selective Hydrogenation of Phenylacetylene. Catal. Letters, 2019, 149(2), 361–372.Filippova A.D., Sozarukova M.M., Baranchikov A.E. et al. Peroxidase-like Activity of CeO2 Nanozymes: Particle Size and Chemical Environment Matter. Molecules, 2023, 28(9), 3811.Filippova A.D., Sozarukova M.M., Baranchikov A.E. et al. Peroxidase-like Activity of CeO2 Nanozymes: Particle Size and Chemical Environment Matter. Molecules, 2023, 28(9), 3811.Sozarukova M.M., Kochneva E.M., Proskurnina E.V. et al. Albumin Retains Its Transport Function after Interaction with Cerium Dioxide Nanoparticles. ACS Biomater. Sci. Eng., 2023, 9(12), 6759–6772.Sozarukova M.M., Kochneva E.M., Proskurnina E.V. et al. Albumin Retains Its Transport Function after Interaction with Cerium Dioxide Nanoparticles. ACS Biomater. Sci. Eng., 2023, 9(12), 6759–6772.Pustulka S.M., Ling K., Pish S.L. et al. Protein Nanoparticle Charge and Hydrophobicity Govern Protein Corona and Macrophage Uptake. ACS Appl. Mater. Interfaces, 2020, 12(43), 48284–48295.Pustulka S.M., Ling K., Pish S.L. et al. Protein Nanoparticle Charge and Hydrophobicity Govern Protein Corona and Macrophage Uptake. ACS Appl. Mater. Interfaces, 2020, 12(43), 48284–48295.Lundqvist M., Stigler J., Elia G. et al. Nanoparticle size and surface properties determine the protein corona with possible implications for biological impacts. Proc. Natl. Acad. Sci., 2008, 105(38), 14265–14270.Lundqvist M., Stigler J., Elia G. et al. Nanoparticle size and surface properties determine the protein corona with possible implications for biological impacts. Proc. Natl. Acad. Sci., 2008, 105(38), 14265–14270.Chaudhary Y.S., Panigrahi S., Nayak S. et al. Facile synthesis of ultra-small monodisperse ceria nanocrystals at room temperature and their catalytic activity under visible light. J. Mater. Chem., 2010, 20(12), 2381.Chaudhary Y.S., Panigrahi S., Nayak S. et al. Facile synthesis of ultra-small monodisperse ceria nanocrystals at room temperature and their catalytic activity under visible light. J. Mater. Chem., 2010, 20(12), 2381.Barth A. The infrared absorption of amino acid side chains. Prog. Biophys. Mol. Biol., 2000, 74(3–5), 141–173.Barth A. The infrared absorption of amino acid side chains. Prog. Biophys. Mol. Biol., 2000, 74(3–5), 141–173.Diaconeasa Z., Barbu-Tudoran L., Coman C. et al. Cerium oxide nanoparticles and its cytotoxicity human lung cancer cells. Rom. Biotechnol. Lett., 2015, 20, 10679.Diaconeasa Z., Barbu-Tudoran L., Coman C. et al. Cerium oxide nanoparticles and its cytotoxicity human lung cancer cells. Rom. Biotechnol. Lett., 2015, 20, 10679.Tang J., Luan F., Chen X. Binding analysis of glycyrrhetinic acid to human serum albumin: Fluorescence spectroscopy, FTIR, and molecular modeling. Bioorg. Med. Chem., 2006, 14(9), 3210–3217.Tang J., Luan F., Chen X. Binding analysis of glycyrrhetinic acid to human serum albumin: Fluorescence spectroscopy, FTIR, and molecular modeling. Bioorg. Med. Chem., 2006, 14(9), 3210–3217.Usoltsev D., Sitnikova V., Kajava A. et al. Systematic FTIR Spectroscopy Study of the Secondary Structure Changes in Human Serum Albumin under Various Denaturation Conditions. Biomolecules, 2019, 9(8), 359.Usoltsev D., Sitnikova V., Kajava A. et al. Systematic FTIR Spectroscopy Study of the Secondary Structure Changes in Human Serum Albumin under Various Denaturation Conditions. Biomolecules, 2019, 9(8), 359.Umezawa M., Itano R., Sakaguchi N. et al. Infrared spectroscopy analysis determining secondary structure change in albumin by cerium oxide nanoparticles. Front. Toxicol., 2023, 5, 1237819.Umezawa M., Itano R., Sakaguchi N. et al. Infrared spectroscopy analysis determining secondary structure change in albumin by cerium oxide nanoparticles. Front. Toxicol., 2023, 5, 1237819.Kogelheide F., Kartaschew K., Strack M. et al. FTIR spectroscopy of cysteine as a ready-to-use method for the investigation of plasma-induced chemical modifications of macromolecules. J. Phys. D. Appl. Phys., 2016, 49(8), 084004.Kogelheide F., Kartaschew K., Strack M. et al. FTIR spectroscopy of cysteine as a ready-to-use method for the investigation of plasma-induced chemical modifications of macromolecules. J. Phys. D. Appl. Phys., 2016, 49(8), 084004.Patel V., Jose L., Philippot G. et al. Fluoride-assisted detection of glutathione by surface Ce3+/Ce4+ engineered nanoceria. J. Mater. Chem. B, 2022, 10(47), 9855–9868.Patel V., Jose L., Philippot G. et al. Fluoride-assisted detection of glutathione by surface Ce3+/Ce4+ engineered nanoceria. J. Mater. Chem. B, 2022, 10(47), 9855–9868.Proskurnina E.V., Sozarukova M.M., Ershova E.S. et al. Lipid Coating Modulates Effects of Nanoceria on Oxidative Metabolism in Human Embryonic Lung Fibroblasts: A Case of Cardiolipin. Biomolecules, 2025, 15(1), 53.Proskurnina E.V., Sozarukova M.M., Ershova E.S. et al. Lipid Coating Modulates Effects of Nanoceria on Oxidative Metabolism in Human Embryonic Lung Fibroblasts: A Case of Cardiolipin. Biomolecules, 2025, 15(1), 53.Yuan D., Shen Z., Liu R. et al. Study on the binding of cerium to bovine serum albumin. J. Biochem. Mol. Toxicol., 2011, 25 (4), 263–268.Yuan D., Shen Z., Liu R. et al. Study on the binding of cerium to bovine serum albumin. J. Biochem. Mol. Toxicol., 2011, 25 (4), 263–268.Simón-Vázquez R., Lozano-Fernández T., Peleteiro-Olmedo M. et al. Conformational changes in human plasma proteins induced by metal oxide nanoparticles. Colloids Surfaces B Biointerfaces, 2014, 113, 198–206.Simón-Vázquez R., Lozano-Fernández T., Peleteiro-Olmedo M. et al. Conformational changes in human plasma proteins induced by metal oxide nanoparticles. Colloids Surfaces B Biointerfaces, 2014, 113, 198–206.Liu W., Rose J., Plantevin S. et al. Protein corona formation for nanomaterials and proteins of a similar size: hard or soft corona? Nanoscale, 2013, 5(4), 1658.Liu W., Rose J., Plantevin S. et al. Protein corona formation for nanomaterials and proteins of a similar size: hard or soft corona? Nanoscale, 2013, 5(4), 1658.Sozarukova M.M., Proskurnina E.V., Baranchikov A.E. et al. Antioxidant Activity of Conjugates of Cerium Dioxide Nanoparticles with Human Serum Albumin Isolated from Biological Fluids. Russ. J. Inorg. Chem., 2023, 68(10), 1495–1502.Sozarukova M.M., Proskurnina E.V., Baranchikov A.E. et al. Antioxidant Activity of Conjugates of Cerium Dioxide Nanoparticles with Human Serum Albumin Isolated from Biological Fluids. Russ. J. Inorg. Chem., 2023, 68(10), 1495–1502.

The authors declare that there are no conflicts of interest present.