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    Effect of interface-active proteins on the salt crystal size in waterborne hybrid materials
    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.
    Wissenschaftlicher Artikel
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      111
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    Surface-initiated ring-opening polymerization of ɛ-caprolactone as a feasible approach to modify flax yarn
    (Elsevier, 2022-01)
    Müller-Hülstede, Julia
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    ; ; ;
    Surface-initiated ring-opening (SI-ROP) polymerization of ɛ-caprolactone is known as possible modification method to increase the hydrophobicity of cellulosic substrates. In this study SI-ROP of ɛ-caprolactone is applied on native and mercerized flax yarn. By use of triazabicyclodecene as catalyst, SI-ROP at room temperature was possible and poly-ɛ-caprolactone (PCL) was linked with a weight content of 4–10% to flax yarns. Besides a lower hydrophilicity an increased surface energy was achieved for PCL modified flax yarn. Furthermore, the positive effect of PCL linkage on the fibers surface regarding adhesion potential to an epoxy matrix was shown via conducting fiber-pull-out tests. After SI-ROP of ɛ-caprolactone on flax fiber surface a reduction of fiber pull-out up to 33% was achieved, evoked by physical improvement e.g. better wettability of fiber with epoxy matrix as well as enhanced crosslinking between the hydroxyl groups of the surface grafted PCL and the epoxy resin.
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      61  30
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    Hofmeister-Driven Ion Pairing in Monovalent Salts Directs Fibrinogen Nanofiber Assembly during Drying
    (ACS Publications, 2025-09) ;
    Malisetty Aparna Sai
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    ; ;
    Aniol, Jonas
    Fibrinogen 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.
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      25