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

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Abstract

We study in situ the kinetics of heat-induced fibrilar aggregation of bovine -lactoglobulin at pH 2.0 and 80 °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 -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
Original languageEnglish
Pages (from-to)084701
Number of pages6
JournalJournal of Chemical Physics
Volume124
DOIs
Publication statusPublished - 2006

Keywords

  • aggregation
  • light

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