Effect of interface-active proteins on the salt crystal size in waterborne hybrid materials
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...
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2021
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oai:doaj.org-article:afbacd8569b143afa62b9846e56381fb2021-11-08T10:56:47ZEffect of interface-active proteins on the salt crystal size in waterborne hybrid materials10.1186/s40563-021-00137-82196-4351https://doaj.org/article/afbacd8569b143afa62b9846e56381fb2021-11-01T00:00:00Zhttps://doi.org/10.1186/s40563-021-00137-8https://doaj.org/toc/2196-4351Abstract 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.Stephani StamboroskiKwasi BoatengWelchy Leite CavalcantiMichael NoeskeVinicius Carrillo BeberKarsten ThielIngo GrunwaldPeter SchiffelsStefan DieckhoffDorothea BrüggemannSpringerOpenarticleProtein-based compositesSodium chlorideBovine serum albuminCollagenFibrinogenCrystallizationChemical technologyTP1-1185DentistryRK1-715ENApplied Adhesion Science, Vol 9, Iss 1, Pp 1-22 (2021) |
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DOAJ |
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DOAJ |
language |
EN |
topic |
Protein-based composites Sodium chloride Bovine serum albumin Collagen Fibrinogen Crystallization Chemical technology TP1-1185 Dentistry RK1-715 |
spellingShingle |
Protein-based composites Sodium chloride Bovine serum albumin Collagen Fibrinogen Crystallization Chemical technology TP1-1185 Dentistry RK1-715 Stephani Stamboroski Kwasi Boateng Welchy Leite Cavalcanti Michael Noeske Vinicius Carrillo Beber Karsten Thiel Ingo Grunwald Peter Schiffels Stefan Dieckhoff Dorothea Brüggemann Effect of interface-active proteins on the salt crystal size in waterborne hybrid materials |
description |
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. |
format |
article |
author |
Stephani Stamboroski Kwasi Boateng Welchy Leite Cavalcanti Michael Noeske Vinicius Carrillo Beber Karsten Thiel Ingo Grunwald Peter Schiffels Stefan Dieckhoff Dorothea Brüggemann |
author_facet |
Stephani Stamboroski Kwasi Boateng Welchy Leite Cavalcanti Michael Noeske Vinicius Carrillo Beber Karsten Thiel Ingo Grunwald Peter Schiffels Stefan Dieckhoff Dorothea Brüggemann |
author_sort |
Stephani Stamboroski |
title |
Effect of interface-active proteins on the salt crystal size in waterborne hybrid materials |
title_short |
Effect of interface-active proteins on the salt crystal size in waterborne hybrid materials |
title_full |
Effect of interface-active proteins on the salt crystal size in waterborne hybrid materials |
title_fullStr |
Effect of interface-active proteins on the salt crystal size in waterborne hybrid materials |
title_full_unstemmed |
Effect of interface-active proteins on the salt crystal size in waterborne hybrid materials |
title_sort |
effect of interface-active proteins on the salt crystal size in waterborne hybrid materials |
publisher |
SpringerOpen |
publishDate |
2021 |
url |
https://doaj.org/article/afbacd8569b143afa62b9846e56381fb |
work_keys_str_mv |
AT stephanistamboroski effectofinterfaceactiveproteinsonthesaltcrystalsizeinwaterbornehybridmaterials AT kwasiboateng effectofinterfaceactiveproteinsonthesaltcrystalsizeinwaterbornehybridmaterials AT welchyleitecavalcanti effectofinterfaceactiveproteinsonthesaltcrystalsizeinwaterbornehybridmaterials AT michaelnoeske effectofinterfaceactiveproteinsonthesaltcrystalsizeinwaterbornehybridmaterials AT viniciuscarrillobeber effectofinterfaceactiveproteinsonthesaltcrystalsizeinwaterbornehybridmaterials AT karstenthiel effectofinterfaceactiveproteinsonthesaltcrystalsizeinwaterbornehybridmaterials AT ingogrunwald effectofinterfaceactiveproteinsonthesaltcrystalsizeinwaterbornehybridmaterials AT peterschiffels effectofinterfaceactiveproteinsonthesaltcrystalsizeinwaterbornehybridmaterials AT stefandieckhoff effectofinterfaceactiveproteinsonthesaltcrystalsizeinwaterbornehybridmaterials AT dorotheabruggemann effectofinterfaceactiveproteinsonthesaltcrystalsizeinwaterbornehybridmaterials |
_version_ |
1718442460051406848 |