Adsorption layer formation in dispersions of protein aggregates

B.A. Noskov, A.G. Bykov, Georgi Gochev, Shi-Yow Lin, Giuseppe Loglio, Reinhard Miller, O.Y. Milyaeva

Результат исследований: Научные публикации в периодических изданияхстатья

Выдержка

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.
Язык оригиналаанглийский
Номер статьи102086
Число страниц12
ЖурналAdvances in Colloid and Interface Science
Том276
Ранняя дата в режиме онлайн14 дек 2019
DOI
СостояниеЭлектронная публикация перед печатью - 14 дек 2019

Отпечаток

Dispersions
proteins
Proteins
Adsorption
adsorption
Surface properties
Kinetics
surface properties
kinetics
Elasticity
Amyloidogenic Proteins
elastic properties
shear
Protein Aggregates
Macromolecules
Rheology
Amyloid
globules
Surface tension
Electrostatics

Цитировать

Noskov, B.A. ; Bykov, A.G. ; Gochev, Georgi ; Lin, Shi-Yow ; Loglio, Giuseppe ; Miller, Reinhard ; Milyaeva, O.Y. / Adsorption layer formation in dispersions of protein aggregates. В: Advances in Colloid and Interface Science. 2020 ; Том 276.
@article{daf62a67a452496a9570e531fc0f5322,
title = "Adsorption layer formation in dispersions of protein aggregates",
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.",
keywords = "Amyloid fibrils, Protein microgels, Liquid-fluid interfaces, Adsorption kinetics, Surface rheology",
author = "B.A. Noskov and A.G. Bykov and Georgi Gochev and Shi-Yow Lin and Giuseppe Loglio and Reinhard Miller and O.Y. Milyaeva",
year = "2019",
month = "12",
day = "14",
doi = "10.1016/j.cis.2019.102086",
language = "English",
volume = "276",
journal = "Advances in Colloid and Interface Science",
issn = "0001-8686",
publisher = "Elsevier",

}

Adsorption layer formation in dispersions of protein aggregates. / Noskov, B.A. ; Bykov, A.G.; Gochev, Georgi; Lin, Shi-Yow; Loglio, Giuseppe; Miller, Reinhard ; Milyaeva, O.Y.

В: Advances in Colloid and Interface Science, Том 276, 102086, 02.2020.

Результат исследований: Научные публикации в периодических изданияхстатья

TY - JOUR

T1 - Adsorption layer formation in dispersions of protein aggregates

AU - Noskov, B.A.

AU - Bykov, A.G.

AU - Gochev, Georgi

AU - Lin, Shi-Yow

AU - Loglio, Giuseppe

AU - Miller, Reinhard

AU - Milyaeva, O.Y.

PY - 2019/12/14

Y1 - 2019/12/14

N2 - 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.

AB - 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.

KW - Amyloid fibrils

KW - Protein microgels

KW - Liquid-fluid interfaces

KW - Adsorption kinetics

KW - Surface rheology

U2 - 10.1016/j.cis.2019.102086

DO - 10.1016/j.cis.2019.102086

M3 - Article

VL - 276

JO - Advances in Colloid and Interface Science

JF - Advances in Colloid and Interface Science

SN - 0001-8686

M1 - 102086

ER -