Adsorption of hen egg-white lysozyme at the air–water interface in presence of sodium dodecyl sulphate

Alahverdjieva, V.S.; Fainerman, V. B.; Aksenenko, E. V.; Leser, Martin E.; Miller, R.

doi:10.1016/j.colsurfa.2007.11.062

Cited by 39 publications

(20 citation statements)

References 33 publications

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“…The theoretical model used to fit the experimental data of adsorption was developed by Fainerman and co-workers originally to explain the experimental surface properties of adsorbed proteins [42][43][44][45]. This model has been applied recently to fit the experimental surface pressure isotherm of several Pluronics at the hexane-water interface assuming that polymers can adsorb in different adsorbed states characterized by their molar area, ω [27].…”

Section: Equilibrium Isothermmentioning

confidence: 99%

Interfacial characterization of Pluronic PE9400 at biocompatible (air–water and limonene–water) interfaces

Pérez-Mosqueda

Maldonado-Valderrama

Ramírez

et al. 2013

Colloids and Surfaces B: Biointerfaces

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Section: Equilibrium Isothermmentioning

confidence: 99%

Interfacial characterization of Pluronic PE9400 at biocompatible (air–water and limonene–water) interfaces

Pérez-Mosqueda

Maldonado-Valderrama

Ramírez

et al. 2013

Colloids and Surfaces B: Biointerfaces

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“…We believe that this closure became possible by the extended upper limit in RH of our HHTDMA system (up to 99.5 %). Discrepancy between the κ measured below and above water saturation in the organic and organic-inorganic mixed particles have been reported in several studies (Song et al, 2017a;Zhao et al, 2016;Hansen et al, 2015;Pajunoja et al, 2015;Whitehead et al, 2014;Alfarra et al, 2013;Dusek et al, 2011;Massoli et al, 2010;Good et al, 2010). Petters et al (2006), Hodas et al (2016), Renbaum-Wolff et al (2016, Rastak et al (2017), andLiu et al (2018) suggested that such discrepancies are expected in systems that undergo LLPS at high RH.…”

Section: Discussionmentioning

confidence: 96%

Water uptake of subpollen aerosol particles: hygroscopic growth, cloud condensation nuclei activation, and liquid–liquid phase separation

et al. 2021

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Abstract. Pollen grains emitted from vegetation can release subpollen particles (SPPs) that contribute to the fine fraction of atmospheric aerosols and may act as cloud condensation nuclei (CCN), ice nuclei (IN), or aeroallergens. Here, we investigate and characterize the hygroscopic growth and CCN activation of birch, pine, and rapeseed SPPs. A high-humidity tandem differential mobility analyzer (HHTDMA) was used to measure particle restructuring and water uptake over a wide range of relative humidity (RH) from 2 % to 99.5 %, and a continuous flow CCN counter was used for size-resolved measurements of CCN activation at supersaturations (S) in the range of 0.2 % to 1.2 %. For both subsaturated and supersaturated conditions, effective hygroscopicity parameters, κ, were obtained by Köhler model calculations. Gravimetric and chemical analyses, electron microscopy, and dynamic light scattering measurements were performed to characterize further properties of SPPs from aqueous pollen extracts such as chemical composition (starch, proteins, DNA, and inorganic ions) and the hydrodynamic size distribution of water-insoluble material. All investigated SPP samples exhibited a sharp increase of water uptake and κ above ∼95 % RH, suggesting a liquid–liquid phase separation (LLPS). The HHTDMA measurements at RH >95 % enable closure between the CCN activation at water vapor supersaturation and hygroscopic growth at subsaturated conditions, which is often not achieved when hygroscopicity tandem differential mobility analyzer (HTDMA) measurements are performed at lower RH where the water uptake and effective hygroscopicity may be limited by the effects of LLPS. Such effects may be important not only for closure between hygroscopic growth and CCN activation but also for the chemical reactivity, allergenic potential, and related health effects of SPPs.

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“…Also, adsorption of lysozyme and protein−surfactant mixtures at the air/water interface has been studied using bubble and drop profile analysis tensiometry and ellipsometry. 16 However, the hydrophobic properties of the oils, which decisively affect protein adsorption, are commonly neglected. It turns out that hydrophobicity, polarity, and chain length of oils govern the adsorption kinetics.…”

Section: Introductionmentioning

confidence: 99%

“…As a result, proteins tend to unfold. Also, adsorption of lysozyme and protein–surfactant mixtures at the air/water interface has been studied using bubble and drop profile analysis tensiometry and ellipsometry . However, the hydrophobic properties of the oils, which decisively affect protein adsorption, are commonly neglected.…”

Section: Introductionmentioning

confidence: 99%

Hydrophobic Interface-Assisted Protein Crystallization: Theory and Experiment

Nanev

Saridakis

Govada

et al. 2019

ACS Appl. Mater. Interfaces

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Macromolecular crystallization is crucial to a large number of scientific fields, including structural biology; drug design, formulation, and delivery; manufacture of biomaterials; and preparation of foodstuffs. The purpose of this study is to facilitate control of crystallization, by investigating hydrophobic interface-assisted protein crystallization both theoretically and experimentally. The application of hydrophobic liquids as nucleation promoters or suppressors has rarely been investigated, and provides an underused avenue to explore in protein crystallization. Theoretically, crystal nucleation is regarded as a two-step process, the first step being a local increase in protein concentration due to its adsorption on the hydrophobic surface. Subsequently, the protein is ordered in a crystal lattice. The energetic aspect of crystal nucleation on water/hydrophobic substance interfaces is approached by calculating the balance between the cohesive energy maintaining integrity of the two-dimensional crystal nucleus and the sum of destructive energies tending to tear up the crystal. This is achieved by comparing the number of bonds shared by the units forming the crystal and the number of unshared (dangling) bonds on the crystal surface pointing toward the solution. The same approach is extended to three-dimensional protein crystal nucleation at water/hydrophobic liquid interfaces. Experimentally, we studied protein crystallization over oils and other hydrophobic liquids (paraffin oil, FC-70 Fluorinert fluorinated oil, and three chlorinated hydrocarbons). Crystallizations of α-lactalbumin and lysozyme are compared, and additional information is acquired by studying α-crustacyanin, trypsin, an insulin analogue, and protein Lpg2936. Depending on the protein type, concentration, and the interface aging time, the proteins exhibit different crystallization propensities depending on the hydrophobic liquid used. Some hydrophobic liquids provoke an increase in the effective supersaturation, which translates to enhancement of crystal nucleation at their interface with the crystallization solution, leading to the formation of crystals.

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Adsorption of hen egg-white lysozyme at the air–water interface in presence of sodium dodecyl sulphate

Cited by 39 publications

References 33 publications

Interfacial characterization of Pluronic PE9400 at biocompatible (air–water and limonene–water) interfaces

Interfacial characterization of Pluronic PE9400 at biocompatible (air–water and limonene–water) interfaces

Water uptake of subpollen aerosol particles: hygroscopic growth, cloud condensation nuclei activation, and liquid–liquid phase separation

Hydrophobic Interface-Assisted Protein Crystallization: Theory and Experiment

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