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-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.
Arnaudov
Luben N
LN
Laboratory of Physical Chemistry and Colloid Science, Wageningen University, Dreijenplein 6, 6700 EK Wageningen, The Netherlands. luben.arnaudov@wur.nl
de Vries
Renko
R
Cohen Stuart
Martien A
MA
D000818:Animals; D002417:Cattle; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007782:Lactoglobulins / Q000737:chemistry*; D009502:Neutrons; D011485:Protein Binding; D053838:Scattering, Small Angle
D007782:Lactoglobulins