%0 journal article
%@ 0014-3057
%A Heyn, T.R., Haramus, V.M., Neumann, H.R., Uttinger, M.J., Guckeisen, T., Heuer, M., Selhuber-Unkel, C., Peukert, W., Keppler, J.K.

%D 2019
%J European Polymer Journal

%P 109211 
%R doi:10.1016/j.eurpolymj.2019.08.038
%T Influence of the polydispersity of pH 2 and pH 3.5 beta-lactoglobulin amyloid fibril solutions on analytical methods
%U https://doi.org/10.1016/j.eurpolymj.2019.08.038
 
%X The pH-value shift resulted in an altered degree of acid hydrolysis which led to dissimilar building blocks of the aggregates (peptides at pH 2, non-hydrolyzed protein at pH 3.5). The respective separated amyloid and non-amyloid fractions showed significantly different size (SAXS, SEC, AUC) and charge properties (Zeta potential) than the whole samples. Strong superposition effects were evident with common analyses such as FTIR, TRP fluorescence and Thioflavin-T. At the same time, structural differences of pH 2 and pH 3.5 aggregates could be presented more clearly.