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These modifications can lead to partial denaturation, exposure of hydrophobic regions, and loss of stability, promoting self-assembly into high-molecular structures. Reversible associations serve regulatory roles: protein stabilization, transient functional inactivation, and generation of biological signals. Irreversible associations result in the formation of stable aggregates constituting pathological hallmarks of amyloidosis and other proteopathies. Although Hb and Mb fibrillization is not part of their physiological function, under oxidative stress, altered pH, high temperatures, or the presence of post-translational modifications, they can adopt amyloid-like structures characterized by cross-\u03b2 conformation. Such aggregates exhibit high resistance to proteolysis and accumulate in tissues. Understanding molecular mechanisms behind Hb and Mb aggregation is critical for the diagnosis and timely therapy of amyloid-related diseases. The stability, regular structure, and biocompatibility of Hb and Mb fibrils make them promising for biomedical applications. Functional nanomaterials based on these fibrils are being developed for high-sensitivity biosensors, bioelectronic devices, and nanocarriers for targeted drug delivery.<\/jats:p>","DOI":"10.3390\/ijms262311700","type":"journal-article","created":{"date-parts":[[2025,12,3]],"date-time":"2025-12-03T10:34:01Z","timestamp":1764758041000},"page":"11700","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Association of Hemoglobin and Myoglobin into Supramolecular Complexes: Significance for Life and Practice"],"prefix":"10.3390","volume":"26","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-9965-093X","authenticated-orcid":false,"given":"Olga V.","family":"Kosmachevskaya","sequence":"first","affiliation":[{"name":"Bach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences, 119071 Moscow, Russia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1320-0792","authenticated-orcid":false,"given":"Natalia N.","family":"Novikova","sequence":"additional","affiliation":[{"name":"National Research Center \u201cKurchatov Institute\u201d, 123182 Moscow, Russia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6625-7373","authenticated-orcid":false,"given":"Alexey F.","family":"Topunov","sequence":"additional","affiliation":[{"name":"Bach Institute of Biochemistry, Research Center of Biotechnology of the Russian Academy of Sciences, 119071 Moscow, Russia"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2025,12,3]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"e09347","DOI":"10.7554\/eLife.09347","article-title":"A pH-driven transition of the cytoplasm from a fluid- to a solid-like state promotes entry into dormancy","volume":"5","author":"Munder","year":"2016","journal-title":"eLife"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"9010","DOI":"10.1021\/acs.chemrev.2c00659","article-title":"When Phased without Water: Biophysics of Cellular Desiccation, from Biomolecules to Condensates","volume":"123","author":"Dorone","year":"2023","journal-title":"Chem. Rev."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"3162","DOI":"10.1002\/1873-3468.13597","article-title":"Stress-Specific Aggregation of Proteins in the Amyloid Bodies","volume":"593","author":"Marijan","year":"2019","journal-title":"FEBS Lett."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"5703","DOI":"10.1038\/s41467-019-13686-1","article-title":"Engineering protein assemblies with allosteric control via monomer fold-switching","volume":"10","author":"Campos","year":"2019","journal-title":"Nat. Commun."},{"key":"ref_5","unstructured":"Walker, H.K., Hall, W.D., and Hurst, J.W. (1990). Red Cell Indices. Clinical Methods: The History, Physical, and Laboratory Examinations, Butterworths. [3rd ed.]."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"206","DOI":"10.1002\/humu.9479","article-title":"HbVar Database of Human Hemoglobin Variants and Thalassemia Mutations: 2007 Update","volume":"28","author":"Giardine","year":"2007","journal-title":"Hum. Mutat."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1038\/s41586-021-03819-2","article-title":"Highly Accurate Protein Structure Prediction with AlphaFold","volume":"596","author":"Jumper","year":"2021","journal-title":"Nature"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"W296","DOI":"10.1093\/nar\/gky427","article-title":"SWISS-MODEL: Homology Modelling of Protein Structures and Complexes","volume":"46","author":"Waterhouse","year":"2018","journal-title":"Nucleic Acids Res."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"8370","DOI":"10.1021\/acs.jpcb.9b06571","article-title":"The enhancement of metal-binding properties in hemoglobin: The role of mild damaging factors","volume":"123","author":"Novikova","year":"2019","journal-title":"J. Phys. Chem. B"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"543","DOI":"10.1134\/S0003683821050100","article-title":"Nonenzymatic reactions in metabolism: Their role in evolution and adaptation","volume":"57","author":"Kosmachevskaya","year":"2021","journal-title":"Appl. Biochem. Microbiol."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1134\/S0003683819020091","article-title":"Binding of erythrocyte hemoglobin to the membrane to realize signal-regulatory function","volume":"55","author":"Kosmachevskaya","year":"2019","journal-title":"Appl. Biochem. Microbiol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"eaaf4382","DOI":"10.1126\/science.aaf4382","article-title":"Liquid Phase Condensation in Cell Physiology and Disease","volume":"357","author":"Shin","year":"2017","journal-title":"Science"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"34","DOI":"10.1016\/j.ceb.2017.02.006","article-title":"Cell Adaptation upon Stress: The Emerging Role of Membrane-less Compartments","volume":"47","author":"Rabouille","year":"2017","journal-title":"Curr. Opin. Cell Biol."},{"key":"ref_14","doi-asserted-by":"crossref","unstructured":"van Tartwijk, F.W., and Kaminski, C.F. (2022). Protein Condensation, Cellular Organization, and Spatiotemporal Regulation of Cytoplasmic Properties. Adv. Biol., 6.","DOI":"10.1002\/adbi.202101328"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1038\/nrm700","article-title":"Stress, order and survival","volume":"3","author":"Minsky","year":"2002","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1016\/j.cell.2013.11.028","article-title":"The bacterial cytoplasm has glass-like properties and is fluidized by metabolic activity","volume":"156","author":"Parry","year":"2014","journal-title":"Cell"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1146\/annurev-cellbio-101011-155841","article-title":"Dynamic reorganization of metabolic enzymes into intracellular bodies","volume":"28","author":"Zhao","year":"2012","journal-title":"Annu. Rev. Cell Dev. Biol."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"5514","DOI":"10.1002\/anie.201806092","article-title":"Infinite assembly of folded proteins in evolution, disease, and engineering","volume":"58","author":"Villegas","year":"2019","journal-title":"Angew. Chem. Int. Ed."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"e02409","DOI":"10.7554\/eLife.02409","article-title":"Filament formation by metabolic enzymes is a specific adaptation to an advanced state of cellular starvation","volume":"3","author":"Petrovska","year":"2014","journal-title":"eLife"},{"key":"ref_20","doi-asserted-by":"crossref","unstructured":"Spinelli, S., Marino, A., Morabito, R., and Remigante, A. (2024). Interplay Between Metabolic Pathways and Increased Oxidative Stress in Human Red Blood Cells. Cells, 13.","DOI":"10.3390\/cells13232026"},{"key":"ref_21","first-page":"287","article-title":"Protein Folding and Misfolding: Mechanism and Principles","volume":"40","author":"Englander","year":"2008","journal-title":"Q. Rev. Biophys."},{"key":"ref_22","doi-asserted-by":"crossref","unstructured":"Uversky, V.N. (2025). Protein Intrinsic Disorder and Adaptation to Extreme Environments: Resilience of Chaos. J. Mol. Biol.","DOI":"10.2139\/ssrn.5393896"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"547","DOI":"10.1021\/acs.chemrestox.2c00032","article-title":"Hormesis: A General Biological Principle","volume":"35","author":"Agathokleous","year":"2022","journal-title":"Chem. Res. Toxicol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"1559325819843376","DOI":"10.1177\/1559325819843376","article-title":"Hormesis Promotes Evolutionary Change","volume":"17","author":"Costantini","year":"2019","journal-title":"Dose-Response"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1126\/science.1169375","article-title":"Protein Dynamism and Evolvability","volume":"324","author":"Tokuriki","year":"2009","journal-title":"Science"},{"key":"ref_26","first-page":"1483","article-title":"How membrane surface affects protein structure","volume":"79","author":"Bychkova","year":"2014","journal-title":"Biochemistry"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"2289","DOI":"10.1016\/j.bpj.2008.11.042","article-title":"Agitation and high ionic strength induce amyloidogenesis of a folded PDZ domain in native conditions","volume":"96","author":"Sicorello","year":"2009","journal-title":"Biophys. J."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"26184","DOI":"10.1039\/C9CP04524D","article-title":"Thermodynamics of amyloid fibril formation from chemical depolymerization","volume":"21","author":"Vettore","year":"2019","journal-title":"Phys. Chem. Chem. Phys."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"975","DOI":"10.1016\/j.molcel.2017.02.018","article-title":"Tardigrades Use Intrinsically Disordered Proteins to Survive Desiccation","volume":"65","author":"Boothby","year":"2017","journal-title":"Mol. Cell"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1017\/S0033583598003400","article-title":"From the globular to the fibrous state: Protein structure and structural conversion in amyloid formation","volume":"31","author":"Sunde","year":"1998","journal-title":"Q. Rev. Biophys."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1098\/rstb.2000.0758","article-title":"The structural basis of protein folding and its links with human disease","volume":"356","author":"Dobson","year":"2001","journal-title":"Philos. Trans. R. Soc. Lond. B Biol. Sci."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"5682","DOI":"10.1093\/emboj\/cdf573","article-title":"The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation","volume":"21","author":"Dobson","year":"2002","journal-title":"EMBO J."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"326","DOI":"10.1021\/bm501521r","article-title":"Stable, metastable, and kinetically trapped amyloid aggregate phases","volume":"16","author":"Miti","year":"2015","journal-title":"Biomacromolecules"},{"key":"ref_34","doi-asserted-by":"crossref","unstructured":"Sirangelo, I., and Iannuzzi, C. (2021). Understanding the role of protein glycation in the amyloid aggregation process. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22126609"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1146\/annurev-biochem-061516-044518","article-title":"Protein misfolding diseases","volume":"86","author":"Hartl","year":"2017","journal-title":"Annu. Rev. Biochem."},{"key":"ref_36","doi-asserted-by":"crossref","unstructured":"Gonzalez-Garcia, M., Fusco, G., and De Simone, A. (2021). Membrane interactions and toxicity by misfolded protein oligomers. Front. Cell Dev. Biol., 9.","DOI":"10.3389\/fcell.2021.642623"},{"key":"ref_37","doi-asserted-by":"crossref","unstructured":"Liu, B., Zhang, H., and Qin, X. (2025). Amyloid Fibrils and Their Applications: Current Status and Latest Developments. Nanomaterials, 15.","DOI":"10.3390\/nano15040255"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1111\/j.1365-2141.2007.06794.x","article-title":"Sickle-cell haemoglobin polymerization: Is it the primary pathogenic event of sickle-cell anaemia?","volume":"139","author":"Vekilov","year":"2007","journal-title":"Br. J. Haematol."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1146\/annurev-biochem-061516-045115","article-title":"Protein misfolding, amyloid formation, and human disease: A summary of progress over the last decade","volume":"86","author":"Chiti","year":"2017","journal-title":"Annu. Rev. Biochem."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"6546","DOI":"10.1002\/adma.201505961","article-title":"Amyloid fibrils as building blocks for natural and artificial functional materials","volume":"28","author":"Knowles","year":"2016","journal-title":"Adv. Mater."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"328","DOI":"10.1126\/science.1173155","article-title":"Functional Amyloids as Natural Storage of Peptide Hormones in Pituitary Secretory Granules","volume":"325","author":"Maji","year":"2009","journal-title":"Science"},{"key":"ref_42","doi-asserted-by":"crossref","unstructured":"Franco, E.M., Alves, L.A., Naveed, H., Freitas, V.A.A., Bastos, D.C., and Mattos-Graner, R.O. (2023). Amyloid Fibrils Produced by Streptococcus sanguinis Contribute to Biofilm Formation and Immune Evasion. Int. J. Mol. Sci., 24.","DOI":"10.3390\/ijms242115686"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"e2304031","DOI":"10.1002\/smll.202304031","article-title":"Spider Silk Protein Forms Amyloid-Like Nanofibrils through a Non-Nucleation-Dependent Polymerization Mechanism","volume":"19","author":"Qi","year":"2023","journal-title":"Small"},{"key":"ref_44","doi-asserted-by":"crossref","unstructured":"Santos, M.R., Henriques, B.J., and Santos, R. (2025). Amyloid-Like Structures in Marine Adhesive Proteins. Mar. Drugs, 23.","DOI":"10.3390\/md23090363"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1111\/exd.12559","article-title":"Amyloids, Melanins and Oxidative Stress in Melanomagenesis","volume":"24","author":"Poe","year":"2015","journal-title":"Exp. Dermatol."},{"key":"ref_46","doi-asserted-by":"crossref","unstructured":"Rabbani, N., and Thornalley, P.J. (2021). Protein glycation\u2014Biomarkers of metabolic dysfunction and early-stage decline in health in the era of precision medicine. Redox Biol., 42.","DOI":"10.1016\/j.redox.2021.101920"},{"key":"ref_47","doi-asserted-by":"crossref","unstructured":"Kosmachevskaya, O.V., Novikova, N.N., and Topunov, A.F. (2021). Carbonyl stress in red blood cells and hemoglobin. Antioxidants, 10.","DOI":"10.3390\/antiox10020253"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"409","DOI":"10.1016\/j.ijbiomac.2021.07.058","article-title":"Methylglyoxal-derived hemoglobin advanced glycation end products induce apoptosis and oxidative stress in human umbilical vein endothelial cells","volume":"187","author":"Lee","year":"2021","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"2480","DOI":"10.1007\/s13361-019-02197-4","article-title":"Comprehensive analysis of protein glycation reveals its potential impacts on protein degradation and gene expression in human cells","volume":"30","author":"Sun","year":"2019","journal-title":"J. Am. Soc. Mass Spectrom."},{"key":"ref_50","doi-asserted-by":"crossref","unstructured":"Sharma, C., and Kim, S.R. (2021). Linking oxidative stress and proteinopathy in Alzheimer\u2019s disease. Antioxidants, 10.","DOI":"10.3390\/antiox10081231"},{"key":"ref_51","first-page":"194","article-title":"Advanced glycation end products and oxidative stress in type 2 diabetes mellitus","volume":"11","author":"Nowotny","year":"2021","journal-title":"Biomolecules"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1016\/j.cbi.2007.11.009","article-title":"The tandem of free radicals and methylglyoxal","volume":"171","author":"Kalapos","year":"2008","journal-title":"Chem.-Biol. Interact."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"1293","DOI":"10.1042\/BST0361293","article-title":"Metal-dependent generation of reactive oxygen species from amyloid proteins implicated in neurodegenerative disease","volume":"36","author":"Allsop","year":"2008","journal-title":"Biochem. Soc. Trans."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"1827","DOI":"10.1073\/pnas.0906852107","article-title":"Metal templated design of protein interfaces","volume":"107","author":"Salgado","year":"2010","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"12026","DOI":"10.1002\/anie.201404272","article-title":"The mechanical role of metal ions in biogenic protein based materials","volume":"53","author":"Degtyar","year":"2014","journal-title":"Angew. Chem. Int. Ed."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"894","DOI":"10.1039\/C3SM52447G","article-title":"Protein cluster formation in aqueous solution in the presence of multivalent metal ions\u2014A light scattering study","volume":"10","author":"Soraruf","year":"2014","journal-title":"Soft Matter"},{"key":"ref_57","unstructured":"Wolf, M. (2015). Effective Interactions in Liquid-Liquid Phase Separated Protein Solutions Induced by Multivalent Ions. [Ph.D. Thesis, Eberhard Karls Universit\u00e4t T\u00fcbingen]."},{"key":"ref_58","doi-asserted-by":"crossref","unstructured":"Jayawardena, N., Kaur, M., Nair, S., Malmstrom, J., Goldstone, D., Negron, L., Gerrar, J.A., and Domigan, L.J. (2017). Amyloid fibrils from hemoglobin. Biomolecules, 7.","DOI":"10.3390\/biom7020037"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"15463","DOI":"10.1073\/pnas.0303758100","article-title":"Myoglobin forms amyloid fibrils by association of unfolded polypeptide segments","volume":"100","author":"Forge","year":"2003","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_60","first-page":"101","article-title":"Tubular polymers of normal human hemoglobin","volume":"59","author":"White","year":"1970","journal-title":"Am. J. Pathol."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"1685","DOI":"10.1002\/bip.1979.360180708","article-title":"Self-association of hemoglobin: A dielectric dispersion study","volume":"18","author":"Desnica","year":"1979","journal-title":"Biopolymers"},{"key":"ref_62","first-page":"371","article-title":"Quaternary structure, hydration, and self-association of hemoglobin. A proton magnetic relaxation study","volume":"11","author":"Pifat","year":"1979","journal-title":"Physiol. Chem. Phys."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1016\/0301-4622(81)85033-8","article-title":"Self-association in highly concentrated solutions of myoglobin: A novel analysis of sedimentation equilibrium of highly nonideal solutions","volume":"14","author":"Minton","year":"1981","journal-title":"Biophys. Chem."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"1499","DOI":"10.1002\/prot.22978","article-title":"Indefinite noncooperative self-association of chicken deoxy hemoglobin D","volume":"79","author":"Rana","year":"2011","journal-title":"Proteins Struct. Funct. Bioinform."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"1073","DOI":"10.1242\/jeb.201.8.1073","article-title":"Self-association, cooperativity and supercooperativity of oxygen binding by hemoglobins","volume":"201","author":"Riggs","year":"1998","journal-title":"J. Exp. Biol."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"4689","DOI":"10.1016\/j.actbio.2010.06.023","article-title":"Fibrillar superstructure formation of hemoglobin A and its conductive, photodynamic and photovoltaic effects","volume":"6","author":"Lee","year":"2010","journal-title":"Acta Biomater."},{"key":"ref_67","doi-asserted-by":"crossref","unstructured":"Bishop, M.F., and Ferrone, F.A. (2023). The sickle-cell fiber revisited. Biomolecules, 13.","DOI":"10.3390\/biom13030413"},{"key":"ref_68","doi-asserted-by":"crossref","unstructured":"Borges da Silva, F.A., Florindo, J.B., Mattos, A.C.d., Costa, F.F., Lorand-Metze, I., and Metze, K. (2024). Accompanying hemoglobin polymerization in red blood cells in patients with sickle cell disease using fluorescence lifetime imaging. Int. J. Mol. Sci., 25.","DOI":"10.20944\/preprints202410.0252.v1"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1110\/ps.062471107","article-title":"Heme binding inhibits the fibrillization of amyloidogenic apomyoglobin and determines lack of aggregate cytotoxicity","volume":"16","author":"Iannuzzi","year":"2007","journal-title":"Protein Sci."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"919","DOI":"10.1107\/S0909049513022772","article-title":"Modulation of the intermolecular interaction of myoglobin by removal of the heme","volume":"20","author":"Imamura","year":"2013","journal-title":"Synchrotron Radiat."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1016\/j.abb.2013.02.019","article-title":"Detection and analysis of protofibrils and fibrils of hemoglobin: Implications for the pathogenesis and cure of heme loss related maladies","volume":"533","author":"Iram","year":"2013","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"299","DOI":"10.1016\/j.biocel.2012.10.004","article-title":"Heme binding site in apomyoglobin may be effectively targeted with small molecules to control aggregation","volume":"45","author":"Shariatizi","year":"2013","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"626","DOI":"10.1016\/j.ijbiomac.2017.09.040","article-title":"Acetylation of lysine residues in apomyoglobin: Structural changes, amyloid fibrillation, and role of surface charge","volume":"107","author":"Meratan","year":"2018","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.saa.2015.10.022","article-title":"Methylglyoxal-induced modification causes aggregation of myoglobin","volume":"155","author":"Banerjee","year":"2016","journal-title":"Spectrochim. Acta Part A Mol. Biomol. Spectrosc."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"115256","DOI":"10.1016\/j.molliq.2020.115256","article-title":"Long-term incubation of myoglobin with glyoxal induces amyloid like aggregation of the heme protein: Implications of advanced glycation end products in protein conformational disorders","volume":"326","author":"Banerjee","year":"2021","journal-title":"J. Mol. Liq."},{"key":"ref_76","doi-asserted-by":"crossref","unstructured":"Iram, A., Alam, T., Khan, J.M., Khan, T.A., Khan, R.H., and Naeem, A. (2013). Molten globule of hemoglobin proceeds into aggregates and advanced glycated end products. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0072075"},{"key":"ref_77","doi-asserted-by":"crossref","unstructured":"Hrynets, Y., Ndagijimana, M., and Betti, M. (2015). Rapid myoglobin aggregation through glucosamine-induced \u03b1-dicarbonyl formation. PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0139022"},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"9712832","DOI":"10.1155\/2018\/9712832","article-title":"Inner-view of nanomaterial incited protein conformational changes: Insights into designable interaction","volume":"2018","author":"Mukhopadhyay","year":"2018","journal-title":"Research"},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1016\/j.nano.2006.07.001","article-title":"Interaction of hemoglobin and copper nanoparticles: Implications in hemoglobinopathy","volume":"2","author":"Bhattacharya","year":"2006","journal-title":"Nanomed. Nanotechnol. Biol. Med."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"892","DOI":"10.1126\/science.8235610","article-title":"Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin","volume":"262","author":"Jennings","year":"1993","journal-title":"Science"},{"key":"ref_81","unstructured":"Wittung-Stafshede, P., and Gomes, C.M. (2010). Folding and assembly of myoglobins and hemoglobins. Protein Folding and Metal Ions: Mechanisms, Biology, Disease, Taylor and Francis, Inc."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1016\/S0076-6879(08)36024-8","article-title":"Spectroscopic and crystallographic characterization of bis-histidyl adducts in tetrameric hemoglobins","volume":"436","author":"Vergara","year":"2008","journal-title":"Methods Enzymol."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"1381","DOI":"10.1016\/j.bpj.2020.01.031","article-title":"The interplay between molten globules and heme disassociation defines human hemoglobin disassembly","volume":"118","author":"Samuel","year":"2020","journal-title":"Biophys. J."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"677","DOI":"10.1016\/S1074-5521(03)00174-1","article-title":"Metal and Redox Modulation of Cysteine Protein Function","volume":"10","author":"Giles","year":"2003","journal-title":"Chem. Biol."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"382","DOI":"10.1161\/CIRCRESAHA.112.268680","article-title":"Cysteine oxidative posttranslational modifications: Emerging regulation in the cardiovascular system","volume":"112","author":"Chung","year":"2013","journal-title":"Circ. Res."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"R84","DOI":"10.1152\/ajpregu.00024.2017","article-title":"Hemoglobin polymerization via disulfide bond formation in the hypoxia-tolerant turtle Trachemys scripta: Implications for antioxidant defense and O2 transport","volume":"314","author":"Petersen","year":"2018","journal-title":"Am. J. Physiol. Regul. Integr. Comp. Physiol."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"e13841","DOI":"10.1111\/apha.13841","article-title":"New insights into survival strategies to oxygen deprivation in anoxia- tolerant vertebrates","volume":"235","author":"Fago","year":"2022","journal-title":"Acta Physiol."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1110\/ps.35702","article-title":"Hemoglobin Porto Alegre forms a tetramer of tetramers superstructure","volume":"11","author":"Fablet","year":"2002","journal-title":"Protein Sci."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1007\/BF00521140","article-title":"Polymeric Hemoglobins of the house mouse (Mus musculus L.): Isolation of cysteinyl peptides","volume":"3","author":"Bonaventura","year":"1969","journal-title":"Biochem. Genet."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"20391","DOI":"10.1074\/jbc.M000373200","article-title":"Reaction of human myoglobin and H2O2: Involvement of a thiyl radical produced at cysteine 110","volume":"275","author":"Witting","year":"2000","journal-title":"J. Biol. Chem."},{"key":"ref_91","first-page":"S180","article-title":"Formation of supplementary metal-binding centers in proteins under stress conditions","volume":"89","author":"Kosmachevskaya","year":"2024","journal-title":"Biochemistry"},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1016\/S0076-6879(08)36025-X","article-title":"Dinitrosyl iron complexes bound with haemoglobin as markers of oxidative stress","volume":"436","author":"Shumaev","year":"2008","journal-title":"Methods Enzymol."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"1645","DOI":"10.1023\/A:1023356221708","article-title":"Coagulation of Zinc-modified Hemoglobin","volume":"72","author":"Khromova","year":"2002","journal-title":"Russ. J. Gen. Chem."},{"key":"ref_94","first-page":"164","article-title":"Zinc ion-mediated concentration of glycated hemoglobin for electrochemical biosensing","volume":"3","author":"Son","year":"2009","journal-title":"BioChip J."},{"key":"ref_95","first-page":"3","article-title":"Opposite effects of electroporation of red blood cell membranes under the influence of zinc ions","volume":"14","author":"Kozlova","year":"2012","journal-title":"Acta Bioeng. Biomech."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"1033","DOI":"10.1039\/c1sc00084e","article-title":"Chemically-controlled supramolecular protein-polymer formed by a myoglobin-based self-assembly system","volume":"2","author":"Oohora","year":"2011","journal-title":"Chem. Sci."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"H549","DOI":"10.1152\/ajpheart.00037.2003","article-title":"A recombinant polymeric hemoglobin with conformational, functional, and physiological characteristics of an in vivo O2 transporter","volume":"285","author":"Bobofchak","year":"2003","journal-title":"Am. J. Physiol. Heart Circ. Physiol."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"927","DOI":"10.1089\/ten.tea.2010.0353","article-title":"Biophysical properties and oxygenation potential of high-molecular-weight glutaraldehyde-polymerized human hemoglobins maintained in the tense and relaxed quaternary states","volume":"17","author":"Zhang","year":"2011","journal-title":"Tissue Eng. Part A"},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1016\/0076-6879(94)31021-1","article-title":"Hemoglobin polymerization","volume":"231","author":"MacDonald","year":"1994","journal-title":"Methods Enzymol."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1080\/10731190009139266","article-title":"Studies on the resuscitative efficacy of polymerized bovine hemoglobin","volume":"28","author":"Bu","year":"2000","journal-title":"Artif. Cells Blood Substit. Immobil. Biotechnol."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1016\/0076-6879(94)31018-1","article-title":"Bis(pyridoxal) polyphosphates as specific intramolecular cross-linking agents for hemoglobin","volume":"231","author":"Benesch","year":"1994","journal-title":"Methods Enzymol."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"953","DOI":"10.1021\/bp0499754","article-title":"Oxidized mono-, di-, tri-, and polysaccharides as potential hemoglobin cross-linking reagents for the synthesis of high oxygen affinity artificial blood substitutes","volume":"20","author":"Eike","year":"2004","journal-title":"Biotechnol. Prog."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1081\/BIO-120037830","article-title":"Hemoglobin polymerized with a naturally occurring crosslinking agent as a blood substitute: In vitro and in vivo studies","volume":"32","author":"Chang","year":"2004","journal-title":"Artif. Cells Blood Substit. Immobil. Biotechnol."},{"key":"ref_104","doi-asserted-by":"crossref","unstructured":"Han, F., Shen, Q., Zheng, W., Zuo, J., Zhu, X., Li, J., Peng, C., Li, B., and Chen, Y. (2023). The Conformational Changes of Bovine Serum Albumin at the Air\/Water Interface: HDX-MS and Interfacial Rheology Analysis. Foods, 12.","DOI":"10.3390\/foods12081601"},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"119445","DOI":"10.1016\/j.ijpharm.2020.119445","article-title":"Damage of proteins at the air\/water interface: Surface tension characterizes globulin interface stability","volume":"584","author":"Xiao","year":"2020","journal-title":"Int. J. Pharm."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"2179","DOI":"10.1039\/b515934b","article-title":"The adsorbed conformation of globular proteins at the air\/water interface","volume":"8","author":"Lad","year":"2006","journal-title":"Phys. Chem. Chem. Phys."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"182","DOI":"10.1007\/s00216-003-1873-6","article-title":"In situ measurement of conformational changes in proteins at liquid interfaces by circular dichroism spectroscopy","volume":"376","author":"Damodaran","year":"2003","journal-title":"Anal. Bioanal. Chem."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"1154","DOI":"10.1016\/j.bpj.2012.01.041","article-title":"Enrichment of Amyloidogenesis at an Air-Water Interface","volume":"102","author":"Jean","year":"2012","journal-title":"Biophys. J."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1042\/BJ20130605","article-title":"The air\u2013water interface determines the outcome of seeding during amyloidogenesis","volume":"456","author":"Trigg","year":"2013","journal-title":"Biochem. J."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"9289","DOI":"10.1021\/acssuschemeng.1c01901","article-title":"Air\u2212Water Interface Assembly of Protein Nanofibrils Promoted by Hydrophobic Additives","volume":"9","author":"Wang","year":"2021","journal-title":"ACS Sustain. Chem. Eng."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"1146","DOI":"10.1038\/s41557-023-01221-1","article-title":"Fibril formation and ordering of disordered FUS LC driven by hydrophobic interactions","volume":"15","author":"Maltseva","year":"2023","journal-title":"Nat. Chem."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"212","DOI":"10.1016\/0021-9797(80)90510-X","article-title":"Oxyhemoglobin A and oxyhemoglobin S films at an air-water interface: Absorption spectra studies","volume":"78","author":"Hirsch","year":"1980","journal-title":"J. Colloid Interface Sci."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1016\/0005-2795(76)90285-3","article-title":"Surface activity of hemoglobin S and other human hemoglobin variants","volume":"427","author":"Elbaum","year":"1976","journal-title":"Biochim. Biophys. Acta (BBA)-Protein Struct."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"10292","DOI":"10.1039\/C6CP08854F","article-title":"Change of the isoelectric point of hemoglobin at the air\/water interface probed by the orientational flip-flop of water molecules","volume":"19","author":"Devineau","year":"2017","journal-title":"Phys. Chem. Chem. Phys."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"e42747","DOI":"10.7554\/eLife.42747","article-title":"Protein denaturation at the air-water interface and how to prevent it","volume":"8","author":"Floris","year":"2019","journal-title":"eLife"},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1246\/bcsj.25.121","article-title":"The structure of surface-denatured protein. IV. The molecular weight, surface area and shape of the surface-denatured hemoglobin molecule","volume":"25","author":"Imahori","year":"1952","journal-title":"Bull. Chem. Soc. Jpn."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"1497","DOI":"10.1177\/00037028211035157","article-title":"Probing the bovine hemoglobin adsorption process and its influence on interfacial water structure at the air-water interface","volume":"75","author":"Chaudhary","year":"2021","journal-title":"Appl. Spectrosc."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"2608","DOI":"10.1073\/pnas.96.6.2608","article-title":"Protein folding at the air\u2014water interface studied with x-ray reflectivity","volume":"96","author":"Gidalevitz","year":"1999","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"12473","DOI":"10.1021\/jp8061288","article-title":"New insight into the surface denaturation of proteins: Electronic sum frequency generation study of cytochrome c at water interfaces","volume":"112","author":"Sen","year":"2008","journal-title":"J. Phys. Chem. B"},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"9385","DOI":"10.1039\/c0cp02277b","article-title":"Interaction of glucose with hemoglobin: A study in aqueous solution and at the air-water interface using the Langmuir-Blodgett technique","volume":"13","author":"Pal","year":"2011","journal-title":"Phys. Chem. Chem. Phys."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"12997","DOI":"10.1039\/c0cp00344a","article-title":"Influence of KCl on the interfacial activity and conformation of hemoglobin studied by Langmuir-Blodgett technique","volume":"12","author":"Mahato","year":"2010","journal-title":"Phys. Chem. Chem. Phys."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"495","DOI":"10.1021\/jp908081r","article-title":"pH induced structural modulation and interfacial activity of hemoglobin at the air\/water interface","volume":"114","author":"Mahato","year":"2010","journal-title":"J. Phys. Chem. B"},{"key":"ref_123","doi-asserted-by":"crossref","unstructured":"Sasso, L., and Gerrard, J.A. (2015). Self-Assembled Biological Nanofibers for Biosensor Applications. Micro and Nanofabrication Using Self-Assembled Biological Nanostructures, Elsevier Inc.. [1st ed.].","DOI":"10.1016\/B978-0-323-29642-7.00001-1"},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"3424","DOI":"10.1002\/adfm.201103054","article-title":"Amyloid directed synthesis of titanium dioxide nanowires and their applications in hybrid photovoltaic devices","volume":"22","author":"Bolisetty","year":"2012","journal-title":"Adv. Funct. Mater."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1002\/btpr.726","article-title":"Amyloid fibrils as functionalizable components of nanocomposite materials","volume":"28","author":"Rao","year":"2012","journal-title":"Biotechnol. Prog."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"204","DOI":"10.1038\/nnano.2010.26","article-title":"Nanostructured films from hierarchical self-assembly of amyloidogenic proteins","volume":"5","author":"Knowles","year":"2010","journal-title":"Nat. Nanotechnol."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"1759","DOI":"10.1002\/btpr.466","article-title":"Nanoporous protein matrix made of amyloid fibrils of \u03b22-microglobulin","volume":"26","author":"Ahn","year":"2010","journal-title":"Biotechnol. Prog."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"5986","DOI":"10.1016\/j.biomaterials.2010.03.080","article-title":"Amyloid hydrogel derived from curly protein fibrils of alpha-synuclein","volume":"31","author":"Bhak","year":"2010","journal-title":"Biomaterials"},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"472","DOI":"10.1002\/adma.201503465","article-title":"Amyloid templated gold aerogels","volume":"28","author":"Nystrom","year":"2016","journal-title":"Adv. Mater."},{"key":"ref_130","doi-asserted-by":"crossref","unstructured":"Casey, C., and Sleator, R.D. (2024). Prions: Structure, function, evolution, and disease. Arch. Microbiol., 207.","DOI":"10.1007\/s00203-024-04200-3"},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1142\/S1793048015300029","article-title":"Protein fibrillar nanopolymers: Molecular-level insights into their structural, physical and mechanical properties","volume":"10","author":"Trusova","year":"2015","journal-title":"Biophys. Rev. Lett."},{"key":"ref_132","doi-asserted-by":"crossref","unstructured":"Hong, S., Choi, D.W., Kim, H.N., Park, C.G., Lee, W., and Park, H.H. (2020). Protein-based nanoparticles as drug delivery systems. Pharmaceutics, 12.","DOI":"10.3390\/pharmaceutics12070604"},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"321","DOI":"10.4155\/tde-2021-0091","article-title":"Protein-based nanomaterials: A new tool for targeted drug delivery","volume":"13","author":"Aljabali","year":"2022","journal-title":"Ther. Deliv."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1016\/j.colsurfa.2012.08.064","article-title":"Hemoglobin\u2013phospholipid interaction and biocomposite formation at air\/water interface","volume":"414","author":"Mahato","year":"2012","journal-title":"Colloids Surf. A Physicochem. Eng. Asp."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1016\/j.tsf.2013.12.052","article-title":"Atomic force microscopy study on the unfolding of globular proteins in the Langmuir films","volume":"552","author":"Furuno","year":"2014","journal-title":"Thin Solid Films"},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"1199","DOI":"10.1021\/jp063377l","article-title":"Interaction of ovalbumin with phospholipids Langmuir\u2013Blodgett film","volume":"111","author":"Kamilya","year":"2007","journal-title":"J. Phys. Chem. B"},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"12775","DOI":"10.1021\/la203053g","article-title":"Protein assembly at the air-water interface studied by fluorescence microscopy","volume":"27","author":"Liao","year":"2011","journal-title":"Langmuir"},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"6477","DOI":"10.1002\/adma.201302283","article-title":"25th anniversary article: What can be done with the Langmuir-Blodgett method? Recent developments and its critical role in materials science","volume":"25","author":"Ariga","year":"2013","journal-title":"Adv. Mater."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"e01038","DOI":"10.1016\/j.heliyon.2018.e01038","article-title":"Unique supramolecular assembly through Langmuir\u2014Blodgett (LB) technique","volume":"4","author":"Hussain","year":"2018","journal-title":"Heliyon"},{"key":"ref_140","doi-asserted-by":"crossref","unstructured":"Gu, W., Li, Q., Wang, R., Zhang, L., Liu, Z., and Jiao, T. (2024). Recent Progress in the Applications of Langmuir\u2013Blodgett Film Technology. Nanomaterials, 14.","DOI":"10.3390\/nano14121039"},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1016\/j.mseb.2009.12.005","article-title":"Developing Langmuir\u2013Blodgett strategies towards practical devices","volume":"169","author":"Zhavnerko","year":"2010","journal-title":"Mater. Sci. Eng. B."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1007\/s12039-013-0370-5","article-title":"Langmuir and Langmuir\u2013Blodgett films of capsules of haemoglobin at air\/water and solid\/air interfaces","volume":"125","author":"Maheshkumar","year":"2013","journal-title":"J. Chem. Sci."},{"key":"ref_143","doi-asserted-by":"crossref","unstructured":"Jiang, Y., Wu, X., Wang, X., Kong, B., Wang, J., and Zhang, H. (2025). Living Hydrogel with Blood Derived Elements for Wound Healing. Mater. Today Bio, 33.","DOI":"10.1016\/j.mtbio.2025.102002"},{"key":"ref_144","doi-asserted-by":"crossref","unstructured":"Jiang, S., Zheng, Y., Xia, H., Liu, Z., Rao, S., Wang, Y., Sun, H., Lu, X., and Xie, C. (2024). Oxygen-Releasing Hydrogels for Tissue Regeneration. Adv. NanoBiomed Res., 4.","DOI":"10.1002\/anbr.202300133"},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"43","DOI":"10.3390\/biochem2010004","article-title":"Heme-Based Gas Sensors in Nature and Their Chemical and Biotechnological Applications","volume":"2","author":"Gondim","year":"2022","journal-title":"BioChem"},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"537","DOI":"10.4314\/bcse.v35i3.6","article-title":"Peroxidase-Like Activity of Hemoglobin-Based Hybrid Materials against Different Substrates and Their Enhanced Application for H2O2 Detection","volume":"35","author":"Altinkaynak","year":"2021","journal-title":"Bull. Chem. Soc. Ethiop."},{"key":"ref_147","doi-asserted-by":"crossref","unstructured":"Sutherland, K., Miller, C., Bassett, A., Cannon, J., Cattron, E., Escobedo, E., Judge, K., Hannesson, M., Johansen, J., and Scott, D. (2025). Substrate Inhibition in Myoglobin and Hemoglobin: Kinetic Insights into Pseudo-Peroxidase Activity. Appl. Chem., 5.","DOI":"10.3390\/appliedchem5030023"},{"key":"ref_148","doi-asserted-by":"crossref","unstructured":"Majid, M.A., Ullah, H., Alshehri, A.M., Tabassum, R., Aleem, A., Khan, A.R., Batool, Z., Nazir, A., and Bibi, I. (2024). Development of Novel Polymer Haemoglobin Based Particles as an Antioxidant, Antibacterial and an Oxygen Carrier Agents. Sci. Rep., 14.","DOI":"10.1038\/s41598-024-53548-5"},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"170293","DOI":"10.1016\/j.cej.2025.170293","article-title":"Hemoglobin-Mediated Synthesis of Iron-Hybridized Gold Nanoclusters for Colorimetric Biosensing and Antibacterial Wound Therapy","volume":"525","author":"Kanwal","year":"2025","journal-title":"Chem. Eng. J."},{"key":"ref_150","doi-asserted-by":"crossref","unstructured":"Penjweini, R., Andreoni, A., Rosales, T., Kim, J., Brenner, M.D., Sackett, D.L., Chung, J.H., and Knutson, J.R. (2018). Intracellular Oxygen Mapping Using a Myoglobin-mCherry Probe with Fluorescence Lifetime Imaging. J. Biomed. Opt., 23.","DOI":"10.1117\/1.JBO.23.10.107001"},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"1611","DOI":"10.1152\/physrev.00031.2023","article-title":"A Versatile Delivery Vehicle for Cellular Oxygen and Fuels or Metabolic Sensor? A Review and Perspective on the Functions of Myoglobin","volume":"104","author":"Adepu","year":"2024","journal-title":"Physiol. Rev."},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"2171","DOI":"10.1021\/jp055301f","article-title":"Fabrication of Electroactive Layer-by-Layer Films of Myoglobin with Gold Nanoparticles of Different Sizes","volume":"110","author":"Zhang","year":"2006","journal-title":"J. Phys. Chem. B"},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1016\/j.jsps.2018.02.005","article-title":"Aggregation and Conformational Stability Evaluation of Myoglobin in the Presence of Ionic Surfactant","volume":"26","author":"Alsenaidy","year":"2018","journal-title":"Saudi Pharm. J."},{"key":"ref_154","first-page":"1575","article-title":"Alternate and Additional Functions of Erythrocyte Hemoglobin","volume":"83","author":"Kosmachevskaya","year":"2018","journal-title":"Biochemistry"},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"734","DOI":"10.1089\/ars.2016.6803","article-title":"Redox and Peroxidase Activities of the Hemoglobin Superfamily: Relevance to Health and Disease","volume":"26","author":"Reeder","year":"2017","journal-title":"Antioxid. Redox Signal."},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"824","DOI":"10.1134\/S0003683825601416","article-title":"Glycation of Leghemoglobin by Methylglyoxal in Comparison with Other Hemoglobins and the Influence on Peroxidase Activity","volume":"61","author":"Nasybullina","year":"2025","journal-title":"Appl. Biochem. Microbiol."},{"key":"ref_157","doi-asserted-by":"crossref","unstructured":"Tuttle, C., Hannesson, M., Henrichsen, A., Hainsworth, L., Condie, C., Whitesides, A., Oren, A., Tanner, S., Terry, B., and Cannon, J. (2025). A Case for Myoglobin \u2212 Macromolecular Rate Theory Applied to Pseudo Peroxidase Kinetics. Biochem. Biophys. Mol. Biol., 13.","DOI":"10.7717\/peerj.19205"},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"2941","DOI":"10.1039\/C4NR06269H","article-title":"Horseradish Peroxidase-Immobilized Magnetic Mesoporous Silica Nanoparticles as a Potential Candidate to Eliminate Intracellular Reactive Oxygen Species","volume":"7","author":"Shen","year":"2015","journal-title":"Nanoscale"},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"3324","DOI":"10.1039\/D3NR05592B","article-title":"Advanced Nanozymes Possess Peroxidase-like Catalytic Activities in Biomedical and Antibacterial Fields: Review and Progress","volume":"16","author":"Ye","year":"2024","journal-title":"Nanoscale"},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"2741","DOI":"10.2174\/092986705774463021","article-title":"Hemoglobin and Myoglobin Associated Oxidative Stress: From Molecular Mechanisms to Disease States","volume":"12","author":"Reeder","year":"2005","journal-title":"Curr. Med. Chem."},{"key":"ref_161","doi-asserted-by":"crossref","unstructured":"Sil, R., and Chakraborti, A.S. (2025). Major Heme Proteins Hemoglobin and Myoglobin with Respect to Their Roles in Oxidative Stress\u2014A Brief Review. Front. Chem., 13.","DOI":"10.3389\/fchem.2025.1543455"},{"key":"ref_162","doi-asserted-by":"crossref","unstructured":"Rerkshanandana, P., Zhao, X., Xiong, Y., Chen, Y., Steffen, A., Chaiwaree, S., Kloypan, C., Pruss, A., Georgieva, R., and B\u00e4umler, H. (2024). Hemoglobin in Submicron Particles (HbMPs) Is Stabilized against Oxidation. Antioxidants, 13.","DOI":"10.3390\/antiox13121477"},{"key":"ref_163","doi-asserted-by":"crossref","unstructured":"Lehn, J.-M. (1995). Supramolecular Chemistry: Concepts and Perspectives, Wiley-VCH.","DOI":"10.1002\/3527607439"},{"key":"ref_164","doi-asserted-by":"crossref","unstructured":"Bozza, M.T., and Jeney, V. (2020). Pro-Inflammatory Actions of Heme and Other Hemoglobin-Derived DAMPs. Front. Immunol., 11.","DOI":"10.3389\/fimmu.2020.01323"},{"key":"ref_165","doi-asserted-by":"crossref","unstructured":"Fu, S., Zhu, X., Huang, F., and Chen, X. (2025). Anti-PEG Antibodies and Their Biological Impact on PEGylated Drugs: Challenges and Strategies for Optimization. Pharmaceutics, 17.","DOI":"10.3390\/pharmaceutics17081074"},{"key":"ref_166","first-page":"1337","article-title":"Plasma Myoglobin Indicates Muscle Damage Associated with Acceleration\/Deceleration during Football","volume":"63","author":"Saita","year":"2023","journal-title":"J. Sports Med. Phys. Fit."},{"key":"ref_167","doi-asserted-by":"crossref","unstructured":"Alanazi, J., Aleanizy, F.S., and Alqahtani, F.Y. (2025). Nanotechnology Approaches for Mitigating Biologic Immunogenicity: A Literature Review. Pharmaceutics, 17.","DOI":"10.3390\/pharmaceutics17070888"}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/26\/23\/11700\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,12,3]],"date-time":"2025-12-03T10:34:33Z","timestamp":1764758073000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/26\/23\/11700"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,12,3]]},"references-count":167,"journal-issue":{"issue":"23","published-online":{"date-parts":[[2025,12]]}},"alternative-id":["ijms262311700"],"URL":"https:\/\/doi.org\/10.3390\/ijms262311700","relation":{},"ISSN":["1422-0067"],"issn-type":[{"type":"electronic","value":"1422-0067"}],"subject":[],"published":{"date-parts":[[2025,12,3]]}}}