Effect of interface-active proteins on the salt crystal size in waterborne hybrid materials

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Abstract

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.

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Stamboroski, S., Boateng, K., Leite Cavalcanti, W., Noeske, M., Beber, V. C., Thiel, K., … Brüggemann, D. (2021). Effect of interface-active proteins on the salt crystal size in waterborne hybrid materials. Applied Adhesion Science, 9(1). https://doi.org/10.1186/s40563-021-00137-8

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