A meta analysis of β-lactoglobulin aggregation kinetics comparing temperature, concentration, and chemistry as modulating influences

Prior published papers has been reanalyzed in this retrospective study of β-lactoglobulin (β-LG) coerced into forming amyloids through assays using both light scattering and Thioflavin T (ThT) fluorescence. The published datasets were extracted and analyzed by a sigmoidal time-dependent model, which yields two time constants which allow comparison between various concentration levels of protein in solution, denaturing temperature, some other additives and the presence of mechanical agitation, however that was accomplished. Shorter aggregation times are observed with increased protein concentration in solution and increased denaturing temperature. The presence of agitation seems to have a large influence and future efforts should be clear to identify the type of agitation if standards are to be developed. Finally comparing scattering and ThT fluorescence, as indicators, it appears that scattering occurs at an earlier time point relative to ThT fluorescence linked with β sheet formation. •Fluorescence precedes scattering as an indicator of aggregate formation.•Higher protein concentration shortens time constants linked with aggregation.•Mixing and turbulence also increase protein-protein interactions.