Ans Fluorescent Probe Induces Clustering of Amyloid Fibers

1-anilino-8-naphthalene sulfonate (ANS) along with thioflavin T (ThT) is a widely used probe for amyloid fibrils detection, however, the mechanism of the dye interaction with fibrils is still not fully understood. Our results indicate that the binding of ANS to amyloid fibrils is due to electrostatic interactions between the dye sulfonate group and cationic groups of amyloid-forming protein. We showed that ANS binding to different types of amyloids accompanying by the significantly increase in the probe fluorescence intensity and leads to changes of the secondary structure of amyloid-forming proteins.