Amyloid diseases, the most clinically relevant protein misfolding pathologies due to the high prevalence of some of them in the population, are characterized by the presence, in specific tissues and organs, of fibrillar deposits of specific peptides or proteins. Increasing efforts are presently dedicated at investigating the structural features and the structure-toxicity relation of the soluble oligomeric precursors arising in the path of fibril formation. In fact, it is increasingly recognised that these unstable, dynamic assemblies are remarkably toxic to cells thus featuring these as the main factor responsible for cell impairment in amyloid diseases. This chapter will review shortly the data presently available on the structural and biochemical features of these assemblies, as well as on their biological and clinical significance.
