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  Adsorption layer formation in dispersions of protein aggregates

Noskov, B., Bykov, A., Gochev, G., Lin, S.-Y., Loglio, G., Miller, R., et al. (2020). Adsorption layer formation in dispersions of protein aggregates. Advances in Colloid and Interface Science, 276: 102086. doi:10.1016/j.cis.2019.102086.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0005-6F8A-4 Version Permalink: http://hdl.handle.net/21.11116/0000-0005-6F8B-3
Genre: Journal Article

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Noskov, B.A., Author
Bykov, A.G., Author
Gochev, G., Author
Lin, S.-Y., Author
Loglio, G., Author
Miller, Reinhard1, Author              
Milyaeva, O.Y., Author
Affiliations:
1Reinhard Miller, Biomaterialien, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863501              

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Free keywords: Amyloid fibrils, Protein microgels, Liquid-fluid interfaces, Adsorption kinetics, Surface rheology
 Abstract: The review discusses recent results on the adsorption of amyloid fibrils and protein microgels at liquid/fluid interfaces. The application of the shear and dilational surface rheology, atomic force microscopy and passive particle probe tracking allowed for elucidating characteristic features of the protein aggregate adsorption while some proposed hypothesis still must be examined by special methods for structural characterization. Although the distinctions of the shear surface properties of dispersions of protein aggregates from the properties of native protein solutions are higher than the corresponding distinctions of the dilational surface properties, the latter ones give a possibility to obtain new information on the formation of fibril aggregates at the water/air interface. Only the adsorption of BLG microgels and fibrils was studied in some details. The kinetic dependencies of the dynamic surface tension and dilational surface elasticity for aqueous dispersions of protein globules, protein microgels and purified fibrils are similar if the system does not contain flexible macromolecules or flexible protein fragments. In the opposite case the kinetic dependencies of the dynamic surface elasticity can be non-monotonic. The solution pH influences strongly the dynamic surface properties of the dispersions of protein aggregates indicating that the adsorption kinetics is controlled by an electrostatic adsorption barrier if the pH deviates from the isoelectric point. A special section of the review considers the possibility to apply kinetic models of nanoparticle adsorption to the adsorption of protein aggregates.

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 Dates: 2019-12-142020
 Publication Status: Published in print
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Title: Advances in Colloid and Interface Science
  Other : Adv. Colloid Interface Sci.
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 276 Sequence Number: 102086 Start / End Page: - Identifier: ISSN: 0001-8686