Abstract
Understanding the molecular process at the basis of polymerization processes of neurotoxic beta-amyloid can give important contributions for designing new therapies for Alzhemier Disease. 

In this perspective, we have performed an in vitro study of the effects on B-amyloid fibrillogenesis of the natural pigment hypericin extracted from Hypericum perforatum (St. John’s worth). Our results show that, thanks to its structural characteristics and peculiar spectroscopic features, hypericin can be easily used to in vitro monitor the appearance of early aggregation states of B-amyloid peptides during the polymerization process and, more importantly, that hypericin can significantly affect and interfere with the early stages of polymerization process, playing the role of an effective aggregation inhibitor.