Resistance of β-Casein at the Air−Water Interface to Enzymatic Cleavage

Lin, Jhih-Min; Ang, Joo Chuan; White, J. W.

doi:10.1021/la103943b

Cited by 3 publications

(3 citation statements)

References 13 publications

(20 reference statements)

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“…Orientation of proteins at air/liquid surfaces due to hydrophilic/phobic interactions can cause changes in orientation and conformation. Lin and coworkers [27] suggested that proteins spontaneously adsorb from aqueous solution to the air/water interface due to the energetically favorable dehydration of hydrophobic regions of the protein surface. Such behavior can be strongly influenced by the protein concentration, secondary structure of the protein, and solution chemistry.…”

Section: Resultsmentioning

confidence: 99%

Vapor conjugation of toluene diisocyanate to specific lysines of human albumin

Hettick

Siegel

Green

et al. 2012

Analytical Biochemistry

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Exposure to toluene diisocyanate (TDI), an industrially important crosslinking agent used in the production of polyurethane products, can cause asthma in sensitive workers. Albumin has been identified as a major reaction target for TDI in vivo, and TDI–albumin reaction products have been proposed to serve as exposure biomarkers and to act as asthmagens, yet they remain incompletely characterized. In the current study, we used a multiplexed tandem mass spectrometry (MS/MS) approach to identify the sites of albumin conjugation by TDI vapors, modeling the air/liquid interface of the lung. Vapor phase TDI was found to react with human albumin in a dose-dependent manner, with up to 18 potential sites of conjugation, the most susceptible being Lys351 and the dilysine site Lys413–414. Sites of vapor TDI conjugation to albumin were quantitatively limited compared with those recently described for liquid phase TDI, especially in domains IIA and IIIB of albumin. We hypothesize that the orientation of albumin at the air/liquid interface plays an important role in vapor TDI conjugation and, thus, could influence biological responses to exposure and the development of in vitro assays for exposure and immune sensitivity.

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Section: Resultsmentioning

confidence: 99%

Vapor conjugation of toluene diisocyanate to specific lysines of human albumin

Hettick

Siegel

Green

et al. 2012

Analytical Biochemistry

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“…The distribution of polar and nonpolar residues has prompted comparison of the adsorption of β-casein in the form of loops and trains with that originally envisaged for polymer chains . The adsorption of β-casein has been extensively studied under a wide variety of conditions. − B-lactoglobulin has a more compact structure due to the presence of disulfide bonds. Hence, β-lactoglobulin has a more well-defined secondary and tertiary structure, and a globular conformation in solution .…”

Section: Introductionmentioning

confidence: 99%

“…have shown how neutron reflectivity, NR, can be used to obtain important information about adsorbed amounts of proteins and the structure of the adsorbed layer at different interfaces. Subsequently the technique of NR has been applied to a variety of different systems. − Building on the application of NR to the study of the adsorption of mixed surfactants and polymer–surfactant mixtures, it has been applied to the study of the adsorption of protein–surfactant mixtures. ,, From these NR measurements and a range of other studies, ,− a relatively clear pattern of behavior has emerged in protein–surfactant mixtures. This involves the possibility of enhanced adsorption due to surface complex formation and competitive adsorption which results in displacement of the protein from the surface at higher surfactant concentrations.…”

Section: Introductionmentioning

confidence: 99%

Adsorption of Hydrophobin–Protein Mixtures at the Air–Water Interface: The Impact of pH and Electrolyte

et al. 2015

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The adsorption of the proteins β-casein, β-lactoglobulin, and hydrophobin, and the protein mixtures of β-casein/hydrophobin and β-lactoglobulin/hydrophobin have been studied at the air-water interface by neutron reflectivity, NR. Changing the solution pH from 7 to 2.6 has relatively little impact on the adsorption of hydrophobin or β-lactoglobulin, but results in a substantial change in the structure of the adsorbed layer of β-casein. In β-lactoglobulin/hydrophobin mixtures, the adsorption is dominated by the hydrophobin adsorption, and is independent of the hydrophobin or β-lactoglobulin concentration and solution pH. At pH 2.6, the adsorption of the β-casein/hydrophobin mixtures is dominated by the hydrophobin adsorption over the range of β-casein concentrations studied. At pH 4 and 7, the adsorption of β-casein/hydrophobin mixtures is dominated by the hydrophobin adsorption at low β-casein concentrations. At higher β-casein concentrations, β-casein is adsorbed onto the surface monolayer of hydrophobin, and some interpenetration between the two proteins occurs. These results illustrate the importance of pH on the intermolecular interactions between the two proteins at the interface. This is further confirmed by the impact of PBS, phosphate buffered saline, buffer and CaCl2 on the coadsorption and surface structure. The results provide an important insight into the adsorption properties of protein mixtures and their application in foam and emulsion stabilization.

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Adsorption of hydrophobin/β-casein mixtures at the solid-liquid interface

Tucker

Petkov

Penfold

et al. 2016

Journal of Colloid and Interface Science

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The adsorption behaviour of mixtures of the proteins β-casein and hydrophobin at the hydrophilic solid-liquid surface have been studied by neutron reflectivity. The results of measurements from sequential adsorption and co-adsorption from solution are contrasted. The adsorption properties of protein mixtures are important for a wide range of applications. Because of competing factors the adsorption behaviour of protein mixtures at interfaces is often difficult to predict. This is particularly true for mixtures containing hydrophobin as hydrophobin possesses some unusual surface properties. At β-casein concentrations ⩾0.1wt% β-casein largely displaces a pre-adsorbed layer of hydrophobin at the interface, similar to that observed in hydrophobin-surfactant mixtures. In the composition and concentration range studied here for the co-adsorption of β-casein-hydrophobin mixtures the adsorption is dominated by the β-casein adsorption. The results provide an important insight into how the competitive adsorption in protein mixtures of hydrophobin and β-casein can impact upon the modification of solid surface properties and the potential for a wide range of colloid stabilisation applications.

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Resistance of β-Casein at the Air−Water Interface to Enzymatic Cleavage

Cited by 3 publications

References 13 publications

Vapor conjugation of toluene diisocyanate to specific lysines of human albumin

Vapor conjugation of toluene diisocyanate to specific lysines of human albumin

Adsorption of Hydrophobin–Protein Mixtures at the Air–Water Interface: The Impact of pH and Electrolyte

Adsorption of hydrophobin/β-casein mixtures at the solid-liquid interface

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