FIGURE 2.

Strain variants of αSyn leading to different clinical phenotypes and possible factors that affect αSyn assembly. We propose the possible mechanisms as to how different αSyn species cause the different types of synucleinopathies. Unstructured αSyn can adopt several structural conformations. Once αSyn forms a structure that favors assembly with each other, it forms fibrils. The final morphology and characters of the fibrils are strongly associated with the initial conformational change. As changing the buffer conditions, such as adding salt or desalting leads to the formation of different types of fibrils, many environmental factors (trans-acting effectors) and some autologous factors (cis-acting effectors) are thought to affect the type of fibril that is formed.