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The intact structure of DBM promotes the transformation of amorphous calcium phosphate (CaP) into dicalcium phosphate dihydrate (DCPD) with a characteristic plate shape and particle size of 5\u201335 \u00b5m. The inclusion of BSA in the coating resulted in a better and more uniform distribution of CaP on the surface of DBM trabeculae. MG63 cells showed that both the obtained forms of CaP and its complex with BSA did not exhibit cytotoxicity up to a concentration of 10 mg\/mL in vitro. Ectopic (subcutaneous) implantation in rats revealed pronounced biocompatibility, as well as strong osteoconductive, osteoinductive, and osteogenic effects for both DBM + CaP and DBM + CaP + BSA, but more pronounced effects for DBM + CaP + BSA. In addition, for the DBM + CaP + BSA samples, there was a pronounced full physiological intrafibrillar biomineralization and proangiogenic effect with the formation of bone-morrow-like niches, accompanied by pronounced processes of intramedullary hematopoiesis, indicating a powerful osteogenic effect of this composite.<\/jats:p>","DOI":"10.3390\/jfb15020027","type":"journal-article","created":{"date-parts":[[2024,1,24]],"date-time":"2024-01-24T04:35:40Z","timestamp":1706070940000},"page":"27","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["Composite Remineralization of Bone-Collagen Matrices by Low-Temperature Ceramics and Serum Albumin: A New Approach to the Creation of Highly Effective Osteoplastic Materials"],"prefix":"10.3390","volume":"15","author":[{"given":"Vladislav V.","family":"Minaychev","sequence":"first","affiliation":[{"name":"Institute of Theoretical and Experimental Biophysics, Russian Academy 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(2021). Functionalization of Synthetic Bone Substitutes. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22094412"},{"key":"ref_2","doi-asserted-by":"crossref","unstructured":"Yang, Y., Chu, C., Xiao, W., Liu, L., Man, Y., Lin, J., and Qu, Y. (2022). Strategies for advanced particulate bone substitutes regulating the osteo-immune microenvironment. Biomed. Mater., 17.","DOI":"10.1088\/1748-605X\/ac5572"},{"key":"ref_3","doi-asserted-by":"crossref","unstructured":"Rodr\u00edguez-Merch\u00e1n, E.C. (2022). Bone Healing Materials in the Treatment of Recalcitrant Nonunions and Bone Defects. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms23063352"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"1724","DOI":"10.1002\/jbm.b.35029","article-title":"A novel classification of bone graft materials","volume":"110","author":"Wickramasinghe","year":"2022","journal-title":"J. Biomed. Mater. Res. B Appl. Biomater."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"529","DOI":"10.1038\/s41580-021-00366-6","article-title":"The principles of directed cell migration","volume":"22","author":"SenGupta","year":"2021","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"166","DOI":"10.1016\/j.jot.2020.01.002","article-title":"Exploratory meta-analysis on dose-related efficacy and complications of rhBMP-2 in anterior cervical discectomy and fusion: 1,539,021 cases from 2003 to 2017 studies","volume":"24","author":"Wen","year":"2020","journal-title":"J. Orthop. Translat."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"1390","DOI":"10.1097\/BRS.0b013e3181a2da08","article-title":"Perioperative complications of recombinant human bone morphogenetic protein-2 on an absorbable collagen sponge versus iliac crest bone graft for posterior cervical arthrodesis","volume":"34","author":"Crawford","year":"2009","journal-title":"Spine"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"43","DOI":"10.3171\/2012.10.SPINE10231","article-title":"Multilevel anterior cervical discectomy and fusion with and without rhBMP-2: A comparison of dysphagia rates and outcomes in 150 patients","volume":"18","author":"Lu","year":"2013","journal-title":"J. Neurosurg. Spine"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"890","DOI":"10.7326\/0003-4819-158-12-201306180-00006","article-title":"Effectiveness and harms of recombinant human bone morphogenetic protein-2 in spine fusion: A systematic review and meta-analysis","volume":"158","author":"Fu","year":"2013","journal-title":"Ann. Intern. Med."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"180","DOI":"10.1016\/j.jocn.2017.06.034","article-title":"Recombinant human bone morphogenetic protein-2 versus iliac crest bone graft in anterior cervical discectomy and fusion: Dysphagia and dysphonia rates in the early postoperative period with review of the literature","volume":"44","author":"Riederman","year":"2017","journal-title":"J. Clin. Neurosci."},{"key":"ref_11","doi-asserted-by":"crossref","unstructured":"Malag\u00f3n-Escand\u00f3n, A., Hautefeuille, M., Jimenez-D\u00edaz, E., Arenas-Alatorre, J., Saniger, J.M., Badillo-Ram\u00edrez, I., Vazquez, N., Pi\u00f1\u00f3n-Zarate, G., and Castell-Rodr\u00edguez, A. (2021). Three-Dimensional Porous Scaffolds Derived from Bovine Cancellous Bone Matrix Promote Osteoinduction, Osteoconduction, and Osteogenesis. Polymers, 13.","DOI":"10.3390\/polym13244390"},{"key":"ref_12","doi-asserted-by":"crossref","unstructured":"Al Qabbani, A., Rani, K.G.A., Syarif, J., AlKawas, S., Sheikh Abdul Hamid, S., Samsudin, A.R., and Azlina, A. (2023). Evaluation of decellularization process for developing osteogenic bovine cancellous bone scaffolds in-vitro. PLoS ONE, 18.","DOI":"10.1371\/journal.pone.0283922"},{"key":"ref_13","first-page":"491","article-title":"Extracellular matrix hydrogel derived from bovine bone is biocompatible in vitro and in vivo","volume":"33","year":"2022","journal-title":"Biomed. Mater. Eng."},{"key":"ref_14","doi-asserted-by":"crossref","unstructured":"Yu, L., and Wei, M. (2021). Biomineralization of Collagen-Based Materials for Hard Tissue Repair. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22020944"},{"key":"ref_15","unstructured":"(2023, June 14). Collagen. Available online: https:\/\/encyclopedia.pub\/entry\/2457."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"e2004418","DOI":"10.1002\/adma.202004418","article-title":"In Vitro Mineralization of Collagen","volume":"33","author":"Oosterlaken","year":"2021","journal-title":"Adv. Mater."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"1513","DOI":"10.1039\/C7CP05261H","article-title":"Structure analysis of collagen fibril at atomic-level resolution and its implications for intra-fibrillar transport in bone biomineralization","volume":"20","author":"Xu","year":"2018","journal-title":"Phys. Chem. Chem. Phys."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1002\/jbm.b.30096","article-title":"Antigenicity and immunogenicity of collagen","volume":"71","author":"Lynn","year":"2004","journal-title":"J. Biomed. Mater. Res. B Appl. Biomater."},{"key":"ref_19","doi-asserted-by":"crossref","unstructured":"Kasravi, M., Ahmadi, A., Babajani, A., Mazloomnejad, R., Hatamnejad, M.R., Shariatzadeh, S., Bahrami, S., and Niknejad, H. (2023). Immunogenicity of decellularized extracellular matrix scaffolds: A bottleneck in tissue engineering and regenerative medicine. Biomater. Res., 27.","DOI":"10.1186\/s40824-023-00348-z"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"110049","DOI":"10.1016\/j.matdes.2021.110049","article-title":"Collagen-based biomaterials for bone tissue engineering","volume":"210","author":"Li","year":"2021","journal-title":"Mater. Des."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"192","DOI":"10.1111\/cid.12274","article-title":"Foreign Body Reaction to Biomaterials: On Mechanisms for Buildup and Breakdown of Osseointegration","volume":"18","author":"Trindade","year":"2016","journal-title":"Clin. Implant Dent. Relat. Res."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"689","DOI":"10.1016\/j.actbio.2021.09.007","article-title":"Biomimetic versus sintered macroporous calcium phosphate scaffolds enhanced bone regeneration and human mesenchymal stromal cell engraftment in calvarial defects","volume":"135","author":"Brennan","year":"2021","journal-title":"Acta Biomater."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"187","DOI":"10.4012\/dmj.2020-001","article-title":"Octacalcium phosphate bone substitute materials: Comparison between properties of biomaterials and other calcium phosphate materials","volume":"39","author":"Suzuki","year":"2020","journal-title":"Dent. Mater. J."},{"key":"ref_24","doi-asserted-by":"crossref","unstructured":"Almulhim, K.S., Syed, M.R., Alqahtani, N., Alamoudi, M., Khan, M., Ahmed, S.Z., and Khan, A.S. (2022). Bioactive Inorganic Materials for Dental Applications: A Narrative Review. Materials, 15.","DOI":"10.3390\/ma15196864"},{"key":"ref_25","doi-asserted-by":"crossref","unstructured":"Fadeeva, I.S., Teterina, A.Y., Minaychev, V.V., Senotov, A.S., Smirnov, I.V., Fadeev, R.S., Smirnova, P.V., Menukhov, V.O., Lomovskaya, Y.V., and Akatov, V.S. (2023). Biomimetic Remineralized Three-Dimensional Collagen Bone Matrices with an Enhanced Osteostimulating Effect. Biomimetics, 8.","DOI":"10.3390\/biomimetics8010091"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"895","DOI":"10.1002\/jbm.a.36867","article-title":"Strontium-substituted biphasic calcium phosphate microspheres promoted degradation performance and enhanced bone regeneration","volume":"108","author":"Chen","year":"2020","journal-title":"J. Biomed. Mater. Res. A"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"A3.B.1","DOI":"10.1002\/0471142735.ima03bs111","article-title":"Trypan Blue Exclusion Test of Cell Viability","volume":"111","author":"Strober","year":"2015","journal-title":"Curr. Protoc. Immunol."},{"key":"ref_28","doi-asserted-by":"crossref","unstructured":"Teterina, A.Y., Minaychev, V.V., Smirnova, P.V., Kobiakova, M.I., Smirnov, I.V., Fadeev, R.S., Egorov, A.A., Ashmarin, A.A., Pyatina, K.V., and Senotov, A.S. (2023). Injectable Hydrated Calcium Phosphate Bone-like Paste: Synthesis, In Vitro, and In Vivo Biocompatibility Assessment. Technologies, 11.","DOI":"10.20944\/preprints202305.1261.v1"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"407","DOI":"10.22203\/eCM.v021a31","article-title":"Osteoinductive biomaterials: Current knowledge of properties, experimental models and biological mechanisms","volume":"21","author":"Barradas","year":"2011","journal-title":"Eur. Cell Mater."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1002\/term.5","article-title":"Osteoinductive biomaterials\u2014Properties and relevance in bone repair","volume":"1","author":"Habibovic","year":"2007","journal-title":"J. Tissue Eng. Regen. Med."},{"key":"ref_31","unstructured":"Lillie, R.D., and Fullmer, H.M. (1976). Histopathologic Technic and Practical Histochemistry, McGraw-Hill."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1016\/j.actbio.2019.12.034","article-title":"The role of calcium phosphate surface structure in osteogenesis and the mechanisms involved","volume":"106","author":"Xiao","year":"2020","journal-title":"Acta Biomater."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"1607","DOI":"10.1002\/jbm.a.36929","article-title":"Precipitation and phase transformation of dicalcium phosphate dihydrate in electrolyte solutions of simulated body fluids: Thermodynamic modeling and kinetic studies","volume":"108","author":"Rabadjieva","year":"2020","journal-title":"J. Biomed. Mater. Res. A"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1002\/jbm.820230603","article-title":"IR spectral changes of bovine serum albumin upon surface adsorption","volume":"23","author":"Lenk","year":"1989","journal-title":"J. Biomed. Mater. Res."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"8572","DOI":"10.1021\/acsomega.9b04421","article-title":"DFT-Calculated IR Spectrum Amide I, II, and III Band Contributions of N-Methylacetamide Fine Components","volume":"5","author":"Ji","year":"2020","journal-title":"ACS Omega"},{"key":"ref_36","doi-asserted-by":"crossref","unstructured":"Alhazmi, H.A. (2019). FT-IR spectroscopy for the identification of binding sites and measurements of the binding interactions of important metal ions with bovine serum albumin. Sci. Pharm., 87.","DOI":"10.3390\/scipharm87010005"},{"key":"ref_37","unstructured":"Picut, C.A. (2016). Atlas of Histology of the Juvenile Rat, Elsevier Inc.. [1st ed.]."},{"key":"ref_38","doi-asserted-by":"crossref","unstructured":"Huang, J.-H., He, H., Chen, Y.-N., Liu, Z., Romani, M.D., Xu, Z.-Y., Xu, Y., and Lin, F.-Y. (2022). Exosomes derived from M2 Macrophages Improve Angiogenesis and Functional Recovery after Spinal Cord Injury through HIF-1\u03b1\/VEGF Axis. Brain Sci., 12.","DOI":"10.3390\/brainsci12101322"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"469","DOI":"10.1007\/s00441-019-03166-9","article-title":"M2 macrophages promote vasculogenesis during retinal neovascularization by regulating bone marrow-derived cells via SDF-1\/VEGF","volume":"380","author":"Wang","year":"2020","journal-title":"Cell Tissue Res."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"1","DOI":"10.22203\/eCM.v024a01","article-title":"In search of an osteoblast cell model for in vitro research","volume":"24","author":"Czekanska","year":"2012","journal-title":"Eur. Cell Mater."},{"key":"ref_41","doi-asserted-by":"crossref","unstructured":"Venkataiah, V.S., Yahata, Y., Kitagawa, A., Inagaki, M., Kakiuchi, Y., Nakano, M., Suzuki, S., Handa, K., and Saito, M. (2021). Clinical Applications of Cell-Scaffold Constructs for Bone Regeneration Therapy. Cells, 10.","DOI":"10.3390\/cells10102687"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"258","DOI":"10.1016\/j.jsb.2013.04.003","article-title":"In vitro models of collagen biomineralization","volume":"183","author":"Nudelman","year":"2013","journal-title":"J. Struct. Biol."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"663","DOI":"10.1038\/nmeth.2938","article-title":"Bone marrow-on-a-chip replicates hematopoietic niche physiology in vitro","volume":"11","author":"Torisawa","year":"2014","journal-title":"Nat. Methods"},{"key":"ref_44","doi-asserted-by":"crossref","unstructured":"Peters, T. (1996). All about Albumin: Biochemistry, Genetics and Medical Applications, Academic Press.","DOI":"10.1016\/B978-012552110-9\/50006-4"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1046\/j.1365-2036.16.s5.2.x","article-title":"Review article: Albumin as a drug\u2014Biological effects of albumin unrelated to oncotic pressure","volume":"16","author":"Evans","year":"2002","journal-title":"Aliment. Pharmacol. Ther."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"314","DOI":"10.1177\/0115426505020003314","article-title":"Albumin therapy in clinical practice","volume":"20","author":"Mendez","year":"2005","journal-title":"Nutr. Clin. Pract."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"643","DOI":"10.1161\/01.RES.32.5.643","article-title":"Transcapillary escape rate of albumin and plasma volume in essential hypertension","volume":"32","author":"Parving","year":"1973","journal-title":"Circ. Res."},{"key":"ref_48","first-page":"H1382","article-title":"Albumin modulation of paracellular permeability of pig vena caval endothelium shows specificity for pig albumin","volume":"264","author":"Vargas","year":"1993","journal-title":"Am. J. Physiol."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"C439","DOI":"10.1152\/ajpcell.1993.265.2.C439","article-title":"Albumin and Ricinus communis agglutinin decrease endothelial permeability via interactions with matrix","volume":"265","author":"Qiao","year":"1993","journal-title":"Am. J. Physiol."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"671","DOI":"10.1194\/jlr.M031336","article-title":"Serum albumin acts as a shuttle to enhance cholesterol efflux from cells","volume":"54","author":"Sankaranarayanan","year":"2013","journal-title":"J. Lipid Res."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"6440","DOI":"10.1073\/pnas.1137188100","article-title":"Structural basis of albumin-thyroxine interactions and familial dysalbuminemic hyperthyroxinemia","volume":"100","author":"Petitpas","year":"2003","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"334","DOI":"10.1053\/j.semperi.2004.09.002","article-title":"Bilirubin-albumin binding and neonatal jaundice","volume":"28","author":"Ahlfors","year":"2004","journal-title":"Semin. Perinatol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"128","DOI":"10.1016\/0167-4838(89)90209-4","article-title":"Bile salts-bovine serum albumin binding: Spectroscopic and thermodynamic studies","volume":"999","author":"Pico","year":"1989","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1097\/MAT.0000000000001720","article-title":"Superior Dialytic Removal of Bilirubin and Bile Acids by Free Fatty Acid Displacement and Its Synergy With Albumin-Based Dialysis","volume":"69","author":"Shi","year":"2023","journal-title":"ASAIO J."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"7674","DOI":"10.1073\/pnas.89.16.7674","article-title":"Nitric oxide circulates in mammalian plasma primarily as an S-nitroso adduct of serum albumin","volume":"89","author":"Stamler","year":"1992","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"300","DOI":"10.2133\/dmpk.24.300","article-title":"Albumin as fatty acid transporter","volume":"24","year":"2009","journal-title":"Drug Metab. Pharmacokinet."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"787","DOI":"10.1080\/15216540500404093","article-title":"The extraordinary ligand binding properties of human serum albumin","volume":"57","author":"Fasano","year":"2005","journal-title":"IUBMB Life"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1002\/prca.200600276","article-title":"Investigation of an albumin-enriched fraction of human serum and its albuminome","volume":"1","author":"Gundry","year":"2007","journal-title":"Proteom. Clin. Appl."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1002\/bmb.2005.494033032470","article-title":"Allosteric modulation of monomeric proteins","volume":"33","author":"Ascenzi","year":"2005","journal-title":"Biochem. Mol. Biol. Educ."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"1783","DOI":"10.1016\/j.febslet.2008.04.057","article-title":"The antioxidant properties of serum albumin","volume":"582","author":"Roche","year":"2008","journal-title":"FEBS Lett."},{"key":"ref_61","doi-asserted-by":"crossref","unstructured":"Belinskaia, D.A., Voronina, P.A., Shmurak, V.I., Jenkins, R.O., and Goncharov, N.V. (2021). Serum Albumin in Health and Disease: Esterase, Antioxidant, Transporting and Signaling Properties. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms221910318"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1006\/abbi.2000.1929","article-title":"Activation of thiol-dependent antioxidant activity of human serum albumin by alkaline pH is due to the B-like conformational change","volume":"380","author":"Lee","year":"2000","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"723","DOI":"10.1042\/bj3380723","article-title":"Phospholipid hydroperoxide cysteine peroxidase activity of human serum albumin","volume":"338","author":"Hurst","year":"1999","journal-title":"Biochem. J."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1016\/j.mam.2011.12.002","article-title":"Human serum albumin: From bench to bedside","volume":"33","author":"Fanali","year":"2012","journal-title":"Mol. Asp. Med."},{"key":"ref_65","first-page":"824","article-title":"The characterization of two specific drug binding sites on human serum albumin","volume":"11","author":"Sudlow","year":"1975","journal-title":"Mol. Pharmacol."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1016\/S0065-3233(08)60640-3","article-title":"Structure of serum albumin","volume":"45","author":"Carter","year":"1994","journal-title":"Adv. Protein Chem."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"1463","DOI":"10.2174\/0929867023369673","article-title":"Reversible and covalent binding of drugs to human serum albumin: Methodological approaches and physiological relevance","volume":"9","author":"Bertucci","year":"2002","journal-title":"Curr. Med. Chem."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1111\/j.1423-0410.2002.tb05326.x","article-title":"Beyond expansion: Structural studies on the transport roles of human serum albumin","volume":"83","author":"Curry","year":"2002","journal-title":"Vox Sang."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"342","DOI":"10.2133\/dmpk.24.342","article-title":"Lessons from the crystallographic analysis of small molecule binding to human serum albumin","volume":"24","author":"Curry","year":"2009","journal-title":"Drug Metab. Pharmacokinet."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"695","DOI":"10.1248\/bpb.25.695","article-title":"Practical aspects of the ligand-binding and enzymatic properties of human serum albumin","volume":"25","author":"Chuang","year":"2002","journal-title":"Biol. Pharm. Bull."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1023\/B:PHAM.0000016241.84630.06","article-title":"Esterase-like activity of serum albumin: Characterization of its structural chemistry using p-nitrophenyl esters as substrates","volume":"21","author":"Sakurai","year":"2004","journal-title":"Pharm. Res."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"464","DOI":"10.1002\/bip.20445","article-title":"Competition of cytarabine and aspirin in binding to serum albumin in multidrug therapy","volume":"81","author":"Bojko","year":"2006","journal-title":"Biopolymers"},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1016\/j.jmb.2005.07.075","article-title":"Structural basis of the drug-binding specificity of human serum albumin","volume":"353","author":"Ghuman","year":"2005","journal-title":"J. Mol. Biol."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"202","DOI":"10.1093\/clinchem\/39.2.202","article-title":"Quantitative analyses of the interaction between calcium ions and human serum albumin","volume":"39","author":"Vorum","year":"1993","journal-title":"Clin. Chem."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"1005","DOI":"10.1016\/j.jinorgbio.2009.04.011","article-title":"Spectroscopic and thermodynamic determination of three distinct binding sites for Co(II) ions in human serum albumin","volume":"103","author":"Bal","year":"2009","journal-title":"J. Inorg. Biochem."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1016\/0040-6031(78)87004-X","article-title":"The binding of Ca2+ and Mg2+ to human serum albumin: A calorimetric study","volume":"25","author":"Eatough","year":"1978","journal-title":"Thermochim. Acta"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"459","DOI":"10.3109\/00365517109095724","article-title":"Binding of calcium to serum albumin. I. Stoichiometry and intrinsic association constant at physiological pH, ionic strength, and temperature","volume":"28","author":"Pedersen","year":"1971","journal-title":"Scand. J. Clin. Lab. Investig."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"174","DOI":"10.1016\/j.molimm.2012.05.011","article-title":"Structural and immunologic characterization of bovine, horse, and rabbit serum albumins","volume":"52","author":"Majorek","year":"2012","journal-title":"Mol. Immunol."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"1282","DOI":"10.1021\/acs.jcim.1c01104","article-title":"Paired Simulations and Experimental Investigations into the Calcium-Dependent Conformation of Albumin","volume":"62","author":"Patel","year":"2022","journal-title":"J. Chem. Inf. Model."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"202","DOI":"10.3390\/ma11020202","article-title":"Microarchitecture of the augmented bone following sinus elevation with an albumin impregnated demineralized freeze-Dried bone allograft (bonealbumin) versus anorganic bovine bone mineral: A randomized prospective clinical, histomorphometric, and micro-Computed tomography study","volume":"11","author":"Orsolya","year":"2018","journal-title":"Materials"},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"356","DOI":"10.1002\/jcb.10510","article-title":"Enhancement of albumin expression in bone tissues with healing rat fractures","volume":"89","author":"Yamaguchi","year":"2003","journal-title":"J. Cell. Biochem."},{"key":"ref_82","first-page":"689","article-title":"Albumin regulates Runx2 and alpha1 (I) collagen mRNA expression in osteoblastic cells: Comparison with insulin-like growth factor-I","volume":"16","author":"Ishida","year":"2005","journal-title":"Int. J. Mol. Med."},{"key":"ref_83","first-page":"1077","article-title":"Role of albumin in osteoblastic cells: Enhancement of cell proliferation and suppression of alkaline phosphatase activity","volume":"14","author":"Ishida","year":"2004","journal-title":"Int. J. Mol. Med."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"6080","DOI":"10.1039\/D0TB01111H","article-title":"Stabilized albumin coatings on engineered xenografts for attenuation of acute immune and inflammatory responses","volume":"8","author":"Tao","year":"2020","journal-title":"J. Mater. Chem. B"},{"key":"ref_85","first-page":"315","article-title":"Serum albumin as a local therapeutic agent in cell therapy and tissue engineering","volume":"43","author":"Simon","year":"2016","journal-title":"BioFactors"},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1002\/jbm.b.33178","article-title":"Cellular internalization and detailed toxicity analysis of protein-immobilized iron oxide nanoparticles","volume":"103","author":"Sanganeria","year":"2015","journal-title":"J. Biomed. Mater. Res. Part B Appl. Biomater."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"108","DOI":"10.1016\/j.jmmm.2018.10.135","article-title":"Human serum albumin as an effective coating for hydrophobic photosensitizes immobilization on magnetic nanoparticles","volume":"475","author":"Ostroverkhov","year":"2019","journal-title":"J. Magn. Magn. Mater."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1163\/156856292X00196","article-title":"Study on the prevention of surface-induced platelet activation by albumin coating","volume":"3","author":"Amiji","year":"1992","journal-title":"J. Biomater. Sci. Polym. Ed."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"416","DOI":"10.1002\/term.2803","article-title":"Serum albumin\u2013coated bone allograft (BoneAlbumin) results in faster bone formation and mechanically stronger bone in aging rats","volume":"13","author":"Schandl","year":"2019","journal-title":"J. Tissue Eng. Regen. Med."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1177\/1553350612451353","article-title":"Albumin-coated bioactive suture for cell transplantation","volume":"20","author":"Weszl","year":"2013","journal-title":"Surg. Innov."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"126","DOI":"10.1002\/jbm.b.33359","article-title":"Serum albumin coating of demineralized bone matrix results in stronger new bone formation","volume":"104","author":"Renner","year":"2016","journal-title":"J. Biomed. Mater. Res. Part B Appl. Biomater."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1016\/j.jmst.2020.02.006","article-title":"In vitro and in vivo biodegradation and biocompatibility of an MMT\/BSA composite coating upon magnesium alloy AZ31","volume":"47","author":"Wang","year":"2020","journal-title":"J. Mater. Sci. Technol."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"228","DOI":"10.1002\/jbm.a.31654","article-title":"Preparation of water-insoluble albumin film possessing nonadherent surface for cells and ligand binding ability","volume":"86","author":"Yamazoe","year":"2008","journal-title":"J. Biomed. Mater. Res. Part A"},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"8402","DOI":"10.1021\/la801221r","article-title":"Facile Cell Patterning on an Albumin-Coated Surface","volume":"24","author":"Yamazoe","year":"2008","journal-title":"Langmuir"},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1002\/jbm.b.30638","article-title":"Adhesion of mouse fibroblasts on hexamethyldisiloxane surfaces with wide range of wettability","volume":"81","author":"Wei","year":"2007","journal-title":"J. Biomed. Mater. Res. Part B Appl. Biomater."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"1233","DOI":"10.1080\/09205063.2012.745717","article-title":"Collagen I gel promotes homogenous osteogenic differentiation of adipose tissue-derived mesenchymal stem cells in serum-derived albumin scaffold","volume":"24","author":"Kang","year":"2013","journal-title":"J. Biomater. Sci. Polym. Ed."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"110678","DOI":"10.1016\/j.msec.2020.110678","article-title":"Albumin-impregnated bone granules modulate the interactions between mesenchymal stem cells and monocytes under in vitro inflammatory conditions","volume":"110","author":"Mijiritsky","year":"2020","journal-title":"Mater. Sci. Eng. C"},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"741","DOI":"10.1007\/s00264-012-1770-8","article-title":"Serum albumin enhances bone healing in a nonunion femoral defect model in rats: A computer tomography micromorphometry study","volume":"37","author":"Skaliczki","year":"2013","journal-title":"Int. Orthop."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"489","DOI":"10.1002\/jor.21527","article-title":"Freeze-dried human serum albumin improves the adherence and proliferation of mesenchymal stem cells on mineralized human bone allografts","volume":"30","author":"Weszl","year":"2012","journal-title":"J. Orthop. Res."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"2097","DOI":"10.1007\/s00264-016-3246-8","article-title":"Bone-Albumin filling decreases donor site morbidity and enhances bone formation after anterior cruciate ligament reconstruction with bone-patellar tendon-bone autografts","volume":"40","author":"Schandl","year":"2016","journal-title":"Int. Orthop."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1556\/OH.2015.30026","article-title":"The use of structural proximal tibial allografts coated with human albumin in treating extensive periprosthetic knee-joint bone deficiency and averting late complications","volume":"156","author":"Janositz","year":"2015","journal-title":"Case Rep. Orv. Hetil."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"297","DOI":"10.11607\/jomi.7554","article-title":"Albumin-Impregnated Allograft Filling of Surgical Extraction Sockets Achieves Better Bone Remodeling Than Filling with Either Blood Clot or Bovine Xenograft","volume":"35","author":"Simonffy","year":"2020","journal-title":"Int. J. Oral Maxillofac. Implants"},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"466","DOI":"10.1016\/j.exger.2010.01.003","article-title":"The sites and topology of mitochondrial superoxide production","volume":"45","author":"Brand","year":"2010","journal-title":"Exp. Gerontol."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"505","DOI":"10.1016\/j.tibs.2010.04.002","article-title":"Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes","volume":"35","author":"Hamanaka","year":"2010","journal-title":"Trends Biochem. Sci."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1186\/1756-8722-6-19","article-title":"Targeting mitochondrial reactive oxygen species as novel therapy for inflammatory diseases and cancers","volume":"6","author":"Li","year":"2013","journal-title":"J. Hematol. Oncol."},{"key":"ref_106","doi-asserted-by":"crossref","unstructured":"Kuten Pella, O., Horny\u00e1k, I., Horv\u00e1thy, D., Fodor, E., Nehrer, S., and Lacza, Z. (2022). Albumin as a Biomaterial and Therapeutic Agent in Regenerative Medicine. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms231810557"},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1007\/s10561-013-9379-8","article-title":"Albumin-coated structural lyophilized bone allografts: A clinical report of 10 cases","volume":"15","author":"Janositz","year":"2014","journal-title":"Cell Tissue Bank."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"236","DOI":"10.1016\/j.colsurfb.2008.01.025","article-title":"MC3T3-E1 cell adhesion to hydroxyapatite with adsorbed bone sialoprotein, bone osteopontin, and bovine serum albumin","volume":"64","author":"Bernards","year":"2008","journal-title":"Colloids Surf. B"},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1146\/annurev.mi.41.100187.002251","article-title":"Bacterial biofilms in nature and disease","volume":"41","author":"Costerton","year":"1987","journal-title":"Annu. Rev. Microbiol."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"380","DOI":"10.1097\/01.mao.0000169767.85549.87","article-title":"Bacterial Adherence to Titanium Surface Coated with Human Serum Albumin","volume":"26","author":"Kinnari","year":"2005","journal-title":"Otol. Neurotol."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"45381","DOI":"10.1021\/acsami.9b15107","article-title":"Albumin Broadens the Antibacterial Capabilities of Nonantibiotic Small Molecule-Capped Gold Nanoparticles","volume":"11","author":"Sun","year":"2019","journal-title":"ACS Appl. Mater. Interfaces"},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"751","DOI":"10.1016\/S0022-5223(19)34297-7","article-title":"Does the addition of albumin to the prime solution in the cardiopulmonary bypass circuit affect clinical outcome? A randomized study","volume":"98","author":"Marelli","year":"1989","journal-title":"J. Thorac. Cardiovasc. Surg."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"128","DOI":"10.1248\/bpb.b16-00867","article-title":"Albumin-Based Nitric Oxide Traffic System for the Treatment of Intractable Cancers","volume":"40","author":"Ishima","year":"2017","journal-title":"Biol. Pharm. Bull."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1002\/jbm.820240203","article-title":"Surface passivation by human albumin of plasmapheresis circuits reduces platelet accumulation and thrombus formation. Experimental and clinical studies","volume":"24","author":"Mulvihill","year":"1990","journal-title":"J. Biomed. Mater. Res."},{"key":"ref_115","first-page":"27","article-title":"ECMO Biocompatibility: Surface Coatings, Anticoagulation, and Coagulation Monitoring","volume":"Volume 3","author":"Firstenberg","year":"2016","journal-title":"Extracorporeal Membrane Oxygenation-Advances in Therapy"},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1097\/00003246-200001000-00012","article-title":"Human neutrophil activation and increased adhesion by various resuscitation fluids","volume":"28","author":"Rhee","year":"2000","journal-title":"Crit. Care Med."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1083\/jcb.122.1.243","article-title":"Albumin inhibits neutrophil spreading and hydrogen peroxide release by blocking the shedding of CD43 (Sialophorin, Leukosialin)","volume":"122","author":"Nathan","year":"1993","journal-title":"J. Cell Biol."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"322","DOI":"10.1590\/S0103-64402011000400011","article-title":"Repair of critical-size defects with autogenous periosteum-derived cells combined with bovine anorganic apatite\/collagen: An experimental study in rat calvaria","volume":"22","author":"Paulo","year":"2011","journal-title":"Braz. Dent. J."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"43425","DOI":"10.1038\/srep43425","article-title":"Comparison of nanoparticular hydroxyapatite pastes of different particle content and size in a novel scapula defect model","volume":"7","author":"Hruschka","year":"2017","journal-title":"Sci. Rep."}],"container-title":["Journal of Functional Biomaterials"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2079-4983\/15\/2\/27\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T13:48:08Z","timestamp":1760104088000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2079-4983\/15\/2\/27"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,1,23]]},"references-count":119,"journal-issue":{"issue":"2","published-online":{"date-parts":[[2024,2]]}},"alternative-id":["jfb15020027"],"URL":"https:\/\/doi.org\/10.3390\/jfb15020027","relation":{},"ISSN":["2079-4983"],"issn-type":[{"value":"2079-4983","type":"electronic"}],"subject":[],"published":{"date-parts":[[2024,1,23]]}}}