Lierath, Jana
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Item type:Publication, Influence of Divalent Metal Ions on the Precipitation of the Plasma Protein Fibrinogen(American Chemical Society, 2021-10-20); ; ; ; Fibrinogen nanofibers are very attractive biomaterials to mimic the native blood clot architecture. Previously, we reported the self-assembly of fibrinogen nanofibers in the presence of monovalent salts and have now studied how divalent salts influence fibrinogen precipitation. Although the secondary fibrinogen structure was significantly altered with divalent metal ions, morphological analysis revealed exclusively smooth fibrinogen precipitates. In situ monitoring of the surface roughness facilitated predicting the tendency of various salts to form fibrinogen fibers or smooth films. Analysis of the chemical composition revealed that divalent salts were removed from smooth fibrinogen films upon rinsing while monovalent Na+ species were still present in fibrinogen fibers. Therefore, we assume that the decisive factor controlling the morphology of fibrinogen precipitates is direct ion–protein contact, which requires disruption of the ion-surrounding hydration shells. We conclude that in fibrinogen aggregates, this mechanism is effective only for monovalent ions, whereas divalent ions are limited to indirect fibrinogen adsorption.journal articleBand:22Heft:1128 22 - Some of the metrics are blocked by yourconsent settings
Item type:Publication, Hofmeister-Driven Ion Pairing in Monovalent Salts Directs Fibrinogen Nanofiber Assembly during Drying(ACS Publications, 2025-09); ; ; Aniol, JonasFibrinogen nanofiber scaffolds hold promise for tissue engineering and wound healing due to their similarity to fibrin clots. We studied how alkaline salts (Na, K) influence fibrinogen precipitation during drying of highly saline dispersions. In situ roughness (Aq) monitoring revealed coprecipitation of salts and fibrinogen. SEM and Aq mapping showed morphologies from smooth (KCl) and faintly fibrous (NaCl) to highly rough and finely fibrous (Na-PO, K-PO). FTIR indicated that secondary structure changes are not always linked to fiber formation. XPS showed a stronger Na uptake, especially with fiber-forming salts. With Na and oxygen-containing polyvalent anions, kosmotropic SO induced fibers, while chaotropic oxalate yielded smooth films. Mg or K with SO did not form any fibers. Molecular dynamics simulations suggest ion-specific binding at the fibrinogen/water interface. We propose a two-dimensional Hofmeister series for tailoring fibrillogenesis via kosmotropic anion-cation pairs, concluding that fiber assembly is salt-driven and governed by cooperative kosmotropic effects.journal articleBand:26Heft:1025