Conformation of β-Lactoglobulin at an Oil/Water Interface as Determined from Proteolysis and Spectroscopic Methods

Dufour, Éric; Dalgalarrondo, Michèle; Adam, L.

doi:10.1006/jcis.1998.5757

Cited by 41 publications

(33 citation statements)

References 37 publications

(44 reference statements)

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“…Considering that these Mabs still bind to BLG at oil/water interfaces, it is concluded that BLG retain a globular conformation interacting by a short region with the oil phase. Similar conclusions were obtained from fluorescence, circular dichroism, and light-scattering experiments (8,26). From light-scattering experiments, it is possible to assess the dimensions of the adsorbed protein layer.…”

Section: Resultssupporting

confidence: 78%

“…Structural studies of β-lactoglobulin (15,16) show that this protein (52% β-sheet and 10% α-helix) has a three-dimensional structure known as a β-barrel, which is shared by a group of proteins capable of transporting small hydrophobic molecules. Upon BLG adsorption at the interface of an oil-in-water emulsion, at least one BLG tryptophan is in a more hydrophobic environment and its secondary structure exhibits a higher helix content as shown by fluorescence and circular dichroism experiments (8).…”

Section: Introductionmentioning

confidence: 98%

“…By comparing the peptides produced during the proteolysis of caseins in solution or adsorbed at the interface, it has been possible to characterize the conformation of these proteins (5)(6)(7). Detailed information on the conformation of adsorbed β-lactoglobulin (BLG) has recently been obtained using proteolysis and spectroscopic methods (8,9). Front-face fluorescence was also used to investigate the modifications of the structure of bovine serum albumin upon its adsorption at the dodecane/water interface (10).…”

Section: Introductionmentioning

confidence: 99%

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Oil/Alkanethiol Layers for the Study of Emulsified Protein Conformation by Surface Plasmon Resonance Using Monoclonal Antibodies

Vénien¹,

Levieux²,

Dufour³

2000

Journal of Colloid and Interface Science

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Section: Resultssupporting

confidence: 78%

Section: Introductionmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

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Oil/Alkanethiol Layers for the Study of Emulsified Protein Conformation by Surface Plasmon Resonance Using Monoclonal Antibodies

Vénien¹,

Levieux²,

Dufour³

2000

Journal of Colloid and Interface Science

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“…CD and fluorescence have also been used to detect a loss of tertiary structure of a-LA upon binding to PS NPs [64]. For b-LG at an oil -water interface, CD measurements indicated an increase in alpha helical content for the adsorbed protein as compared with that in solution [65], with similar results obtained using Fourier transform infrared (FT-IR) spectroscopy [66]. Although it is clear that the function of a-LA is to promote the production of lactose in milk, no clear function has been identified for b-LG.…”

Section: Introductionmentioning

confidence: 99%

The effect of nanoscale surface curvature on the oligomerization of surface-bound proteins

Kurylowicz

Paulin

Mogyoros

et al. 2014

J. R. Soc. Interface.

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ReviewCite this article: Kurylowicz M, Paulin H, Mogyoros J, Giuliani M, Dutcher JR. 2014 The effect of nanoscale surface curvature on the oligomerization of surface-bound proteins. J. R. Soc. The influence of surface topography on protein conformation and association is used routinely in biological cells to orchestrate and coordinate biomolecular events. In the laboratory, controlling the surface curvature at the nanoscale offers new possibilities for manipulating protein-protein interactions and protein function at surfaces. We have studied the effect of surface curvature on the association of two proteins, a-lactalbumin (a-LA) and b-lactoglobulin (b-LG), which perform their function at the oil-water interface in milk emulsions. To control the surface curvature at the nanoscale, we have used a combination of polystyrene (PS) nanoparticles (NPs) and ultrathin PS films to fabricate chemically pure, hydrophobic surfaces that are highly curved and are stable in aqueous buffer. We have used single-molecule force spectroscopy to measure the contour lengths L c for a-LA and b-LG adsorbed on highly curved PS surfaces (NP diameters of 27 and 50 nm, capped with a 10 nm thick PS film), and we have compared these values in situ with those measured for the same proteins adsorbed onto flat PS surfaces in the same samples. The L c distributions for b-LG adsorbed onto a flat PS surface contain monomer and dimer peaks at 60 and 120 nm, respectively, while a-LA contains a large monomer peak near 50 nm and a dimer peak at 100 nm, with a tail extending out to 200 nm, corresponding to higher order oligomers, e.g. trimers and tetramers. When b-LG or a-LA is adsorbed onto the most highly curved surfaces, both monomer peaks are shifted to much smaller values of L c . Furthermore, for b-LG, the dimer peak is strongly suppressed on the highly curved surface, whereas for a-LA the trimer and tetramer tail is suppressed with no significant change in the dimer peak. For both proteins, the number of higher order oligomers is significantly reduced as the curvature of the underlying surface is increased. These results suggest that the surface curvature provides a new method of manipulating protein-protein interactions and controlling the association of adsorbed proteins, with applications to the development of novel biosensors.

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“…However, hydrolysis provides a useful means for studying the topography of proteins at an oil-water interface. In this way, the structures of α s1 -casein (14,15), β-casein (13,(16)(17)(18)(19), and β-lactoglobulin (20,21) adsorbed at the surface of oil droplets in emulsion have been largely studied. The caseins with random coil structure can spread widely over the interface, whereas spreading is lower in the case of more-rigid proteins, such as whey proteins.…”

Section: Introductionmentioning

confidence: 99%

Dilational Rheology of Mixed β-Casein/Tween 20 and β-Casein (f114–169)/Tween 20 Films at Oil–Water Interface

Girardet

Humbert

Creusot³

et al. 2001

Journal of Colloid and Interface Science

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Conformation of β-Lactoglobulin at an Oil/Water Interface as Determined from Proteolysis and Spectroscopic Methods

Cited by 41 publications

References 37 publications

Oil/Alkanethiol Layers for the Study of Emulsified Protein Conformation by Surface Plasmon Resonance Using Monoclonal Antibodies

Oil/Alkanethiol Layers for the Study of Emulsified Protein Conformation by Surface Plasmon Resonance Using Monoclonal Antibodies

The effect of nanoscale surface curvature on the oligomerization of surface-bound proteins

Dilational Rheology of Mixed β-Casein/Tween 20 and β-Casein (f114–169)/Tween 20 Films at Oil–Water Interface

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