Multiscale insights into fibroblast growth factor 23 adsorption on polyelectrolyte layers: From molecular properties to biointerfaces

  • Fibroblast growth factor 23 (FGF23) is a clinically significant protein hormone regulating phosphate and vitamin D metabolism, with elevated levels linked to chronic kidney disease, cardiovascular disorders, and impaired bone homeostasis. Despite its relevance as both a biomarker and a therapeutic target, its interactions with functional biomaterials remain poorly understood. In this work, we investigate the FGF23 adsorption on polyelectrolyte layers using a combination of theoretical modeling and experimental methods. Theoretical calculations provided insights into the protein's charge distribution and diffusion properties, while experimental measurements quantified its hydrodynamic diameter, electrophoretic mobility, and electrokinetic charge over a broad range of pH values. Microscale thermophoresis revealed quantitative binding affinities of FGF23 to hyaluronic acid, chitosan, and poly(diallyldimethylammonium chloride). Adsorption studies on mica, silica, and polyelectrolyte mono-Fibroblast growth factor 23 (FGF23) is a clinically significant protein hormone regulating phosphate and vitamin D metabolism, with elevated levels linked to chronic kidney disease, cardiovascular disorders, and impaired bone homeostasis. Despite its relevance as both a biomarker and a therapeutic target, its interactions with functional biomaterials remain poorly understood. In this work, we investigate the FGF23 adsorption on polyelectrolyte layers using a combination of theoretical modeling and experimental methods. Theoretical calculations provided insights into the protein's charge distribution and diffusion properties, while experimental measurements quantified its hydrodynamic diameter, electrophoretic mobility, and electrokinetic charge over a broad range of pH values. Microscale thermophoresis revealed quantitative binding affinities of FGF23 to hyaluronic acid, chitosan, and poly(diallyldimethylammonium chloride). Adsorption studies on mica, silica, and polyelectrolyte mono- and bilayers showed that FGF23 binds to both negatively and positively charged substrates, with binding affinities following: hyaluronic acid < poly(diallyldimethylammonium chloride) < chitosan. Desorption occurred more readily from negatively charged surfaces (mica, silica and hyaluronic acid), indicating weaker interactions compared to positively charged layers. These results reveal fundamental aspects of protein –polyelectrolyte interactions and highlight the reversible binding capacity of FGF23 to negatively charged surfaces. Such adsorption behavior provides a physicochemical framework for considering FGF23-polyelectrolyte systems in the design of therapeutic carriers and bioactive materials. However, any direct relevance to wound healing, chronic kidney disease, or cardiovascular disorders remains prospective and requires dedicated biological validation.zeige mehrzeige weniger

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Autor*innen:A. Pomorska Gawel, M. Dąbkowska, D. Kosior, P. Batys, A. Szatanik, Julia Witt, Özlem Özcan SandikciogluORCiD, A. Michna
Dokumenttyp:Zeitschriftenartikel
Veröffentlichungsform:Verlagsliteratur
Sprache:Englisch
Titel des übergeordneten Werkes (Englisch):International Journal of Biological Macromolecules
Jahr der Erstveröffentlichung:2026
Organisationseinheit der BAM:6 Materialchemie
6 Materialchemie / 6.2 Material- und Oberflächentechnologien
Verlag:Elsevier B.V.
Jahrgang/Band:341
Ausgabe/Heft:Part 1
Aufsatznummer:150221
Erste Seite:1
Letzte Seite:14
DDC-Klassifikation:Technik, Medizin, angewandte Wissenschaften / Ingenieurwissenschaften / Ingenieurwissenschaften und zugeordnete Tätigkeiten
Freie Schlagwörter:Adsorption; Binding affinity; Molecular dynamics; Stability; Streaming potential measurements
Themenfelder/Aktivitätsfelder der BAM:Material
Material / Advanced Materials
DOI:10.1016/j.ijbiomac.2026.150221
ISSN:0141-8130
Verfügbarkeit des Dokuments:Datei im Netzwerk der BAM verfügbar ("Closed Access")
Datum der Freischaltung:28.01.2026
Referierte Publikation:Ja
Datum der Eintragung als referierte Publikation:28.01.2026
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