Noeske, Paul-Ludwig Michael
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Noeske, Paul-Ludwig Michael
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Noeske, Paul-Ludwig Michael
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Item type:Publication, Effect of interface-active proteins on the salt crystal size in waterborne hybrid materials(SpringerOpen, 2021); ; ; ; Aqueous processes yielding hybrid or composite materials are widespread in natural environments and their control is fundamental for a multiplicity of living organisms. Their design and in vitro engineering require knowledge about the spatiotemporal evolution of the interactions between the involved liquid and solid phases and, especially, the interphases governing the development of adhesion during solidification. The present study illustrates the effects of distinct proteins on the precipitation of sodium chloride encompassing the size, shape and distribution of halite crystals formed during the drying of droplets containing equally concentrated saline protein solutions. The precipitates obtained from aqueous sodium chloride formulations buffered with tris(hydroxymethyl)aminomethane (Tris) contained either bovine serum albumin (BSA), fibrinogen or collagen and were characterized with respect to their structure and composition using optical and electron microscopy as well as x-ray analysis. The acquired findings highlight that depending on the protein type present during droplet drying the halite deposits predominantly exhibit cubic or polycrystalline dendritic structures. Based on the phenomenological findings, it is suggested that the formation of the interphase between the growing salt phase and the highly viscous saline aqueous jelly phase containing protein governs not only the material transport in the liquid but also the material exchange between the solid and liquid phases.journal articleBand:9Heft:7111 - Some of the metrics are blocked by yourconsent settings
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