Thermodynamics, adsorption kinetics and rheology of mixed protein–surfactant interfacial layers

Kotsmar, Csaba; Pradines, Vincent; Alahverdjieva, V.S.; Aksenenko, E. V.; Fainerman, V. B.; Kovalchuk, V. I.; Krägel, J.; Leser, Martin E.; Noskov, Boris A.; Miller, R.

doi:10.1016/j.cis.2009.05.002

Cited by 193 publications

(187 citation statements)

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“…and PAK3 molecules, as has been previously reported for interactions between proteins and surfactants 25,26 . To test this hypothesis, ELP5 and PAK3 solutions were mixed below the T t (4 °C), which resulted in a disordered white viscous aggregate ( Supplementary Fig.…”

Section: Resultssupporting

confidence: 55%

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Co-assembly, spatiotemporal control and morphogenesis of a hybrid protein–peptide system

et al. 2015

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ature uses self-assembly to create a widespread variety of complex structures with elaborate geometries and outstanding properties 1 such as hierarchical order, adaptability, selfhealing and bioactivity. Developing new bioinspired processes based on dynamic self-assembly could facilitate the fabrication of synthetic three-dimensional (3D) materials with enhanced complexity, dynamic properties and functionality 2 . Proteins are particularly attractive building blocks because of their versatility and biofunctionality 3 . Elastin-like polypeptides (ELPs) 4 are recombinant proteins that have generated great interest 5 as a result of their modular structure, bioactivity, ease of design and production, and the possibility to create robust and elastic materials 5,6 . ELPs allow for a tunable molecular design 7 and are based on the tropoelastin recurrent motif Val-Pro-Gly-X-Gly (VPGXG), in which X is any amino acid other than proline 7 . This repeating pentapeptide provides ELPs with a thermoresponsive behaviour. Below a critical transition temperature (T t ), the ELP molecule undergoes a reversible-phase transition wherein the protein is soluble in aqueous solution and becomes highly solvated, surrounded by clatharate-like water structures. Above the T t , the hydrophobic domains dehydrate and the protein chain hydrophobically collapses and aggregates to form a phaseseparated state 8 .The use of natural and synthetic proteins to create functional materials has been hindered by the difficulty in controlling their conformation and nanoscale assembly with the precision required to form macroscopic materials. This limitation has driven the development of simpler and more-predictable peptide-based materials 9,10 . Peptide amphiphiles (PAs), for example, are synthetic molecules that can self-assemble into nanofibres and create functional 3D hydrogels that emulate the fibrous architecture of the extracellular matrix (ECM) 11,12 . Nonetheless, most peptide and/or protein materials are formed through equilibrium-based self-assembly approaches that are capable of generating stable supramolecular structures, but with limited hierarchy and spatiotemporal control, which has hindered their functionality 2 .Novel approaches based on the dynamic self-assembly of inorganic building blocks [13][14][15] , actin self-organization 16 and the combination of top-down processes with peptide self-assembly have been reported recently 17 . In particular, Stupp and co-workers have described a self-assembling membrane system obtained through strong electrostatic interactions between PAs and oppositely charged polysaccharides 18 . However, the possibility to exploit the unique structural and functional properties of proteins to create dynamic hierarchical materials remains an elusive target. In this study, we attempt to overcome this hurdle by using self-assembling peptides to promote protein conformational changes and guide their assembly into complex, yet functional, materials. We report the discovery and development of a protein/peptide system t...

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Section: Resultssupporting

confidence: 55%

“…The ELP molecules at the air-water interface could enhance the membrane adhesion at the point of contact with the interface (Supplementary Fig. 13) 25,26 . Growth of the tubular structures can be triggered simply by displacing the interface.…”

Section: Resultsmentioning

confidence: 99%

Co-assembly, spatiotemporal control and morphogenesis of a hybrid protein–peptide system

et al. 2015

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“…The presence of an apparent yield stress in the bulk rheological measurement is also reported for solutions of ovalbumin 22 , saliva 23 , monoclonal antibodies 24 and acacia gum 25 . In practice, the interfacial contribution from surface-active components in multicomponent fluids can be suppressed by the addition of a low molecular-weight mobile surfactant, which competes with the protein for adsorption onto the interface 2,11,[26][27][28][29][30] . The irreversibility of the adsorption, the presence of heterogeneous domains, significant interfacial phase separation at the interface and the sensitivity of the structure of the interfacial layer to the adsorption history make accurate measurements a challenging task 3,4,31 .…”

Section: Introductionmentioning

confidence: 99%

“…Multicomponent mixtures of proteins and surfactants are used in many of these applications, and are also commonly found in many biological systems [6][7][8] including blood: a mixture of serum albumins along with various other surface-active components 6,8 . The addition of surfactants to protein solutions can substantially modify the physiochemical properties of the resulting interface 2,6,[9][10][11] . For example, the interfacial shear viscos- ity (which characterizes resistance to changes in shape at constant area on a two-dimensional interface), is affected by the structure, composition and conformation of the interfacial components of these mixed systems 3,6,9,10,12 .…”

Section: Introductionmentioning

confidence: 99%

Interfacial viscoelasticity, yielding and creep ringing of globular protein–surfactant mixtures

2011

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Protein-surfactant mixtures arise in many industrial and biological systems, and indeed, blood itself is a mixture of serum albumins along with various other surface-active components. Bovine serum albumin (BSA) solutions, and globular proteins in general, exhibit an apparent yield stress in bulk rheological measurements at surprisingly low concentrations. By contrasting interfacial rheological measurements with corresponding interface-free data obtained using a microfluidic rheometer, we show that the apparent yield stress exhibited by these solutions arises from the presence of a viscoelastic layer formed due to the adsorption of protein molecules at the air-water interface. The coupling between instrument inertia and surface elasticity in a controlled stress device also results in a distinctive damped oscillatory strain response during creep experiments known as"creep ringing". We show that this response can be exploited to extract the interfacial storage and loss moduli of the protein interface. The interfacial creep response at small strains can be described by a simple second order system, such as the linear Jeffreys model, however the interfacial response rapidly becomes nonlinear beyond strains of order 1%. We use the two complementary techniques of interfacial rheometry and microfluidic rheometry to examine the systematic changes in the surface and bulk material functions for mixtures of a common non-ionic surfactant, Polysorbate 80, and BSA. It is observed that the nonlinear viscoelastic properties of the interface are significantly suppressed by the presence of even a relatively small amount of surfactant (c surf > 10 −3 wt.%).

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“…В свою очередь, лазерное облучение при ЭВЛК гипотетически способно существенно влиять . При заболеваниях артериальных сосудов пока-зано, что если успешного лечения не происходит, то измененные показатели ПВ и ПУ положительной ди-намики не претерпевают [14]. Как демонстрирует многофакторный дисперсион-ный анализ, влияние мощности лазерного излучения при выполнении ЭВЛК у пациентов с ВБ мало воз-действует на интегральную динамику физико-хими-ческих показателей АРСК.…”

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Adsorption-rheological properties of blood in patients with varicose vein during surgical treatment

Syniachenko

Samoilenko

2017

UJS

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Thermodynamics, adsorption kinetics and rheology of mixed protein–surfactant interfacial layers

Cited by 193 publications

References 84 publications

Co-assembly, spatiotemporal control and morphogenesis of a hybrid protein–peptide system

Co-assembly, spatiotemporal control and morphogenesis of a hybrid protein–peptide system

Interfacial viscoelasticity, yielding and creep ringing of globular protein–surfactant mixtures

Adsorption-rheological properties of blood in patients with varicose vein during surgical treatment

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