Timon R. Heyn

TL;DR: Different morphologies of amyloid aggregates of beta-lactoglobulin were prepared by incubation at pH 2 or pH 3.5 for up to 72 h and the building blocks at both pH values changed towards smaller peptides.

TL;DR: In this paper, 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.

TL;DR: Two recombinant beta-lactoglobulin (BLG) B variants were produced in E. coli and production/isolation resulted in native BLG without post-translational modifications, showing similar emulsifying properties to natural BLGs.

TL;DR: In this paper, the authors identify critical factor combinations of pH, temperature, stirring speed, protein and ion concentration that specifically affect the lag-, and growth phase of beta-lactoglobulin amyloid aggregation.

TL;DR: In this article, conditions under which amyloid-like aggregates are formed and their impact on aggregate morphology are identified and summarized, where the focus is on β-lactoglobulin, but generic effects on other proteins are discussed.