Kinetics of adsorption of proteins and surfactants

Miller, R.; Fainerman, V. B.; Leser, Martin E.; Michel, Martin

doi:10.1016/j.cocis.2004.08.002

Cited by 60 publications

(47 citation statements)

References 46 publications

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“…This is because binding of non-ionic surfactant to protein can strengthen the protein network. [2]. Thermodynamic models which allow a quantitative description of the adsorption of protein [23] and protein-surfactant mixed films from the aqueous bulk phase into liquid interfaces can be well described by recently proposed models [2], which assume multiple states of the protein molecule in the surface layer and internal compressibility of the surfactant surface layer [24 • ].…”

Section: Adsorption Isothermmentioning

confidence: 99%

Physico-chemical properties of surfactant and protein films

Patino

Niño

Sánchez

2007

Current Opinion in Colloid & Interface Science

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Section: Adsorption Isothermmentioning

confidence: 99%

Physico-chemical properties of surfactant and protein films

Patino

Niño

Sánchez

2007

Current Opinion in Colloid & Interface Science

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“…β-casein is one of the most frequently investigated model proteins [24][25][26] and the non-ionic alkyl dimethyl phosphine oxides represent an excellent model surfactants for fundamental investigations [27]. The formation of mixed surface layers formed by proteins and surfactants was the example studied in [18,22,[28][29][30][31].…”

Section: Introductionmentioning

confidence: 99%

“…3), the process lasts about 600 s. On the contrary, the simultaneous adsorption from mixed solutions is by orders of magnitude faster. A quantitative description for both adsorption protocols requires modification of the available theoretical models [28].…”

mentioning

confidence: 99%

Drop profile analysis tensiometry with drop bulk exchange to study the sequential and simultaneous adsorption of a mixed β-casein /C12DMPO system

et al. 2008

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The formation of mixed protein/surfactant adsorption layers is studied by the drop profile analysis tensiometry equipped with a special tool for drop volume exchange during experiments. This arrangement allows investigating in the traditional way by simultaneous adsorption from a mixed solution and also by a subsequent adsorption of the protein followed by surfactant. The experiments are performed for β-casein as the protein in the presence of different amounts of the non-ionic surfactant C 12 DMPO. The surface layers formed via the two routes show similar equilibrium surface properties. However, the dynamics of desorption of the protein complexes into the pure buffer solution deviate significantly, which is explained by the different locations of the protein/surfactant interaction. Although in both cases the complex formation is based on hydrophobic interaction, the accessibility of the hydrophobic parts of pre-adsorbed proteins due to unfolding is more favourable by the surfactant than in the solution bulk. Therefore, the amount desorbed from surface layers formed from mixed solutions is significantly less as compared to the displacement of proteins by subsequently injected surfactants interacting at the surface.

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“…For example, some detergents cause proteins to adsorb to the fluid interface. 21, 22 To avoid these potential problems, we have chosen to eliminate coalescence by preventing direct contact of adjacent reagent plugs.…”

Section: Introductionmentioning

confidence: 99%

Using Three-Phase Flow of Immiscible Liquids To Prevent Coalescence of Droplets in Microfluidic Channels: Criteria To Identify the Third Liquid and Validation with Protein Crystallization

Chen

Reyes

et al. 2007

Langmuir

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This manuscript describes the effect of interfacial tensions on three-phase liquid-liquid-liquid flow in microfluidic channels and the use of this flow to prevent microfluidic plugs from coalescing. One problem in using microfluidic plugs as microreactors is the coalescence of adjacent plugs caused by the relative motion of plugs during flow. Here, coalescence of reagent plugs was eliminated by using plugs of a third immiscible liquid as spacers to separate adjacent reagent plugs. This work tested the requirements of interfacial tensions for plugs of a third liquid to be effective spacers. Two candidates satisfying the requirements were identified, and one of these liquids was used in the crystallization of protein human Tdp1 to demonstrate its compatibility with protein crystallization in plugs. This method for identifying immiscible liquids for use as a spacer will also be useful for applications involving manipulation of large arrays of droplets in microfluidic channels.

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Kinetics of adsorption of proteins and surfactants

Cited by 60 publications

References 46 publications

Physico-chemical properties of surfactant and protein films

Physico-chemical properties of surfactant and protein films

Drop profile analysis tensiometry with drop bulk exchange to study the sequential and simultaneous adsorption of a mixed β-casein /C12DMPO system

Using Three-Phase Flow of Immiscible Liquids To Prevent Coalescence of Droplets in Microfluidic Channels: Criteria To Identify the Third Liquid and Validation with Protein Crystallization

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