In: Soft Matter, 2011, vol. 7, p. 8127-8134
We report the first direct, non-invasive experimental evidence of a 2D isotropic–nematic transition for highly anisotropic nanoparticles at liquid–liquid interfaces by using passive fluorescent particle tracking. In order to illustrate the potential of this approach on systems of high real practical and biological relevance, we select as a model anisotropic nanoparticles β-lactoglobulin...
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In: Langmuir, 2010, vol. 26, no. 19, p. 15366–15375
Interfacial properties of native β-lactoglobulin monomers and their heat-induced fibers, of two different lengths, were investigated at pH 2, through surface tension measurements at water−air and water−oil interfaces and interfacial shear rheology at the water−oil interface. The applied heat treatment generates a mixed system of fibers with unconverted monomers and hydrolyzed peptides. The...
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In: Nature Nanotechnology, 2010, vol. 5, p. 423 - 428
The aggregation of proteins is central to many aspects of daily life, including food processing, blood coagulation, eye cataract formation disease and prion-related neurodegenerative infections. However, the physical mechanisms responsible for amyloidosis—the irreversible fibril formation of various proteins that is linked to disorders such as Alzheimer's, Creutzfeldt–Jakob and Huntington's...
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In: Langmuir, 2010, vol. 26, no. 13, p. 10401–10405
We investigate the effects of variable linear charge density and Debye length on the mesoscopic properties of β-lactoglobulin fibers in water, by changing the pH and ionic strength, respectively. We determine the isotropic−nematic (I−N) transition by cross-polarized microscopy and quantify by atomic force microscopy the increasing tendency of the fibers to aggregate upon raising ionic...
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In: Langmuir, 2010, vol. 26, no. 1, p. 504–514
We have developed a new method allowing the study of the thermodynamic phase behavior of mesoscopic colloidal systems consisting of amyloid protein fibers in water, obtained by heat denaturation and aggregation of β-lactoglobulin, a dairy protein. The fibers have a cross section of about 5.2 nm and two groups of polydisperse contour lengths: (i) long fibers of 1−20 μm, showing semiflexible...
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In: Biomacromolecules, 2008, vol. 9, no. 9, p. 2477–2486
We report on the conformation of heat-induced bovine β-lactoglobulin (βlg) aggregates prepared at different pH conditions, and their complexes with model anionic surfactants such as sodium dodecyl sulfate (SDS). The investigation was carried out by combining a wide range of techniques such as ultra small angle light scattering, static and dynamic light scattering, small angle neutron...
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