Rheological properties of protein films

Murray, Brent S.

doi:10.1016/j.cocis.2010.06.005

Cited by 169 publications

(108 citation statements)

References 120 publications

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“…While nearly no sub-phase corrections are required for the data measured using the DWR geometry, in other instruments used for making interfacial measurements with lower characteristic values of the Boussinesq numbers, the sub-phase contributions to the torque must be carefully accounted for (see, for example, the papers by Mannheimer and Schechter 33 and Oh and Slattery 34 . Several studies 3,4,31,35 have noted the long time scales required for adsorbed interfacial layers to reach equilibrium, with Wierenga et al 35 waiting for as long as 24 hours. This effect is even more pronounced in surfactant-protein mixtures 31,36 .…”

Section: Methodsmentioning

confidence: 99%

“…The addition of surfactants can modify the microstructure, equilibrium and dynamic adsorption values, and the rheological characteristics of interfacial layers 3,10,11,55 and the interfacial properties of the mixed protein/surfactant system are also quite different from the bulk. Studies of the microstructure at the interface using Brewster Angle Microscopy or Fluorescence Microscopy [56][57][58] or by evaluating local dynamics using micro-rheology reveal the presence of considerable interfacial phase separation with localized surfactant-rich and protein-rich regions 3,4,36 .…”

Section: Protein-surfactant Mixturesmentioning

confidence: 99%

“…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 . Given these challenges, a simple experimental protocol that provides a check for the presence of surface viscoelasticity and an estimate of its magnitude in protein-surfactant mixtures will be of broad utility.…”

Section: Introductionmentioning

confidence: 99%

“…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 . In this study, we focus on the interfacial and bulk rheology of a proteinsurfactant mixture, using solutions of a model globular protein, Bovine Serum Albumin (BSA), mixed with a non-ionic surfactant polysorbate 80 (or Tween 80 TM ).…”

Section: Introductionmentioning

confidence: 99%

“…The dynamic interfacial properties of these adsorbed interfacial layers are important for a number of technological applications including foam and emulsion formation and stabilization in food processing 3,4 , cosmetics and pharmaceutical industry 4,5 . The interfacial viscoelasticity also plays an important role in spray coating, Langmuir-Blodgett deposition, liquid-liquid deposition, two phase flows and mass transfer 1,2 .…”

Section: Introductionmentioning

confidence: 99%

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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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Section: Methodsmentioning

confidence: 99%

Section: Protein-surfactant Mixturesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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

2011

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Synthesis and Manipulation of Colloid and Interface Structure and Properties by Exposure to Perfluorocarbon Gases

Krafft

2022

Patai's Chemistry of Functional Groups

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This chapter exposes the notion of physical reactivity of chemically inert nonfunctional compounds and the decisive role it can play in the synthesis of colloids and interfaces and in controlling their properties. Thus, introduction of perfluorocarbon vapor in the atmosphere above an aqueous dispersion of phospholipids promotes the adsorption of the latter to the air/water interface. When contacted with a monolayer of dipalmitoylphosphatidylcholine, perfluorocarbons fluidize this monolayer, inhibiting the formation of the ordered semicrystalline phase upon compression. Perfluorohexane can help desorb serum albumin from a phospholipid film, allowing the phospholipid to respread upon expansion. The perfluorocarbon also effectively counteracts lung surfactant deactivation by serum proteins. Exposure to perfluorohexane gas of a monolayer of phospholipids spread on aqueous solutions of C 2 F 5 ‐labeled molecules prompts their selective adsorption into the interfacial film. When the phospholipid forms liquid‐condensed monolayers, the C 2 F 5 ‐labeled species remain partially trapped in the monolayer after the perfluorohexane is removed. Perfluorocarbons can also impact the behavior of nanoparticles. Thus, nanodiamond clusters are efficiently disaggregated, which promotes their adsorption to the air/water interface, thereby enabling the formation of perfluorocarbon‐stabilized, nanodiamond‐shelled microbubbles. Prospective applications include lung surfactant substitutes that resist deactivation by serum proteins for treating lung conditions, novel drug‐loaded medical microbubbles, and nanodiamond‐based microbubbles for multimodal diagnostic and delivery purposes.

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Thermodynamics and Kinetics of Mixed Protein/Surfactant Adsorption Layers at Liquid Interfaces

Miller

Aksenenko

Alahverdjieva³

et al. 2013

Proteins in Solution and at Interfaces

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Rheological properties of protein films

Cited by 169 publications

References 120 publications

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

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

Synthesis and Manipulation of Colloid and Interface Structure and Properties by Exposure to Perfluorocarbon Gases

Thermodynamics and Kinetics of Mixed Protein/Surfactant Adsorption Layers at Liquid Interfaces

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