Dilational Viscoelasticity of Proteins Solutions in Dynamic Conditions

被引：20

作者：

Fainerman, Valentin B. ^{[1
]}

Kovalchuk, Volodymyr I. ^{[2
]}

Aksenenko, Eugene V. ^{[3
]}

Zinkovych, Igor I. ^{[4
]}

Makievski, Alexander V. ^{[1
]}

Nikolenko, Mykola V. ^{[5
]}

Miller, Reinhard ^{[6
]}

机构：

[1] SINTERFACE Technol, D-12489 Berlin, Germany

[2] Inst Biocolloid Chem, UA-03142 Kiev, Ukraine

[3] Inst Colloid Chem & Chem Water, UA-03680 Kiev, Ukraine

[4] Maxim Gorki Donetsk Natl Med Univ, UA-25015 Kirovohrad, Ukraine

[5] Ukrainian State Univ Chem Technol, UA-49005 Dnipro, Ukraine

[6] MPI Colloids & Interfaces, D-14476 Potsdam, Germany

来源：

LANGMUIR | 2018年 / 34卷 / 23期

关键词：

AIR-WATER-INTERFACE; SURFACE DILATATIONAL RHEOLOGY; PROFILE ANALYSIS TENSIOMETRY; HEXADECANE/WATER INTERFACE; BETA-LACTOGLOBULIN; FLEXIBLE PROTEINS; ADSORPTION; LAYERS; DROP; THERMODYNAMICS;

D O I：

10.1021/acs.langmuir.8b00631

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Drop profile analysis tensiometry used in the oscillating drop mode provides the dilational viscoelasticity of adsorption layers at liquid interfaces. Applied during the progress of adsorption the dynamic surface rheology can be monitored. For beta-casein solutions at the same surface pressure values, the larger the dynamic dilational viscoelasticity the longer the adsorption time, i.e., the smaller the studied protein concentration is. For beta-lactoglobulin and human serum albumin, the differences in the viscoelasticity values are less or not dependent on the adsorption time at identical surface pressures. The observed effects are caused by the flexibility of BCS, while the globular proteins BLG and HSA do not change their conformation significantly within the adsorption layer.

引用

页码：6678 / 6686

页数：9

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