Time-resolved small-angle neutron scattering during heat-induced fibril formation from bovine beta-lactoglobulin

We study in situ the kinetics of heat-induced fibrilar aggregation of bovine beta-lactoglobulin at pH 2.0 and 80 degrees C for the first time by time-resolved small-angle neutron scattering. A simple model for the scattering from a mixture of monodisperse charged spheres (monomeric beta-lactoglobuli...

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Bibliographic Details
Published inThe Journal of chemical physics Vol. 124; no. 8; p. 084701
Main Authors Arnaudov, Luben N, de Vries, Renko, Cohen Stuart, Martien A
Format Journal Article
LanguageEnglish
Published United States 28.02.2006
Subjects
Animals
Cattle
Hot Temperature
Hydrogen-Ion Concentration
Lactoglobulins - chemistry
Neutrons
Protein Binding
Scattering, Small Angle
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Summary:We study in situ the kinetics of heat-induced fibrilar aggregation of bovine beta-lactoglobulin at pH 2.0 and 80 degrees C for the first time by time-resolved small-angle neutron scattering. A simple model for the scattering from a mixture of monodisperse charged spheres (monomeric beta-lactoglobulin) interacting via a screened electrostatic repulsion and noninteracting long cylinders (protein fibrils) is used to describe the data. The experimental data are fitted to the model and the concentration of the monomeric protein and the protein incorporated in fibrils are obtained as adjustable parameters. Thus, a simple physical model allows the determination of realistic kinetic parameters during fibrilar protein aggregation. This result constitutes an important step in understanding the process of irreversible fibrilar aggregation of proteins.
ISSN:0021-9606
DOI:10.1063/1.2171418