Impact Of Hofmeister Series Anion On Amyloid Fibrillation

In the 1880 s,Czech scientist Hofmeister discovered a series of salts that have consistent effects on the solubility and stability of proteins.Now,this salt series is the well-known Hofmeister series.In recent years,scientists began to investigate the impact of Hofmeister ions on protein aggregation.In this study,we will use ThT fluorescence assay and atomic force microscopy(AFM)to investigate the Hofmeister anions on lysozyme fibrillation under different concentration and pH conditions.We chose six anions from the Hofmeister series and hen egg white lysozyme as the model protein.We use ThT fluorescence assay to study the kinetic of lysozyme fibrillation and use curve-fitting to extract kinetic paramters.We use AFM to study the morphology of lysozyme fibrils.Kinetic investigation shows that the impacts of these Hofmeister series anions do not follow their orders in the Hofmeister series regardless of concentration;and under different pH conditions,higher pH results in longer lag phase.AFM results show that different Hofmeiser ions have different impacts on the morphology of lysozyme fibrils;the same anion has similar impact on fibril morphology regardless of concentration;the impact of Hofmeister series ions on fibril morphology is independent of pH and dependent on the type of anion.