**8. Conclusions**

In this chapter, we have presented the state-of-the-art for the field of α-synuclein structure, and for its fibril formation and interactions with membranes. There are still many unanswered questions regarding the correlation between α-synuclein membrane affinity, and its function and its role in synucleinopathies. As the disruption of membranes by αsynuclein correlates with the binding affinity of α-synuclein for particular membrane compositions and with the induced helical conformation of α-synuclein, this suggests that inappropriate membrane permeabilization is the cause of cell dysfunction, and even cell death, in amyloid diseases. Protofibrillar or fibrillar α-synuclein results in a much more rapid destruction of membranes than soluble monomeric α-synuclein, which indicates that protofibrils or fibrils are likely to be significantly neurotoxic. Further studies of α-synuclein interactions with membranes are still very important to provide us with a fuller undertanding of the molecular mechanisms of its implications in Parkinson's disease.
