Figure 2
![αSyn can be divided into three regions: the repeat rich N-terminal region, the hydrophobic, aggregation-prone, non-amyloid component (NAC), both of which contain imperfect KTKEGV repeat regions (N1–N7), and the highly charged, intrinsically disordered, C-terminal region. This latter region can be a hotspot for proteolytic cleavage. Asn103 can be cleaved by AEP and cathepsin L [58,61], Glu114 is a target for calpain-1, cathepsin B, cathepsin K, and cathepsin L [55,59,66,67], Asn122 can be cleaved by AEP, calpain-1, cathepsin B, and cathepsin L [55,59,66,67], while cleavage after Ala124 is a target for cathepsin D [59]. Created with BioRender.com.](https://port.silverchair-cdn.com/port/content_public/journal/essaysbiochem/65/7/10.1042_ebc20210028/1/ebc-2021-0028ci002.png?Expires=1716456551&Signature=3SXy9nbL6cr0KqbEGA2UvQgVTGAzGWPHjlpKWIjNZRv~3fR8VjB84T4vsh26-QmTl2WDTK67VvyZ3wTibLTpuuy~-HiCbJ0w2-txtjyfhHF-wrrmo7trPaltcJ5jpzpCyW~-i9dhbcQt1xQB1-gOyT6QAwohLr3303V94TgNA3wj9dpC~IF4fDn1ts1daUaGWQQLWpYDRNT9OR1010wgrm08-7GbjL7AanQoBrot6Hv7sEUWahN9q-kHd99Na2abNktRGN93riHPy5qs4edY3d4z~VTmO573I6NWzJgUI8f3wiM9ClobCvG-rFK-Co8DU~Zgs8oQFQV3qlaVHsJJag__&Key-Pair-Id=APKAIE5G5CRDK6RD3PGA)
Schematic of αSyn and some of the major proteolytic cleavage sites
αSyn can be divided into three regions: the repeat rich N-terminal region, the hydrophobic, aggregation-prone, non-amyloid component (NAC), both of which contain imperfect KTKEGV repeat regions (N1–N7), and the highly charged, intrinsically disordered, C-terminal region. This latter region can be a hotspot for proteolytic cleavage. Asn103 can be cleaved by AEP and cathepsin L [58,61], Glu114 is a target for calpain-1, cathepsin B, cathepsin K, and cathepsin L [55,59,66,67], Asn122 can be cleaved by AEP, calpain-1, cathepsin B, and cathepsin L [55,59,66,67], while cleavage after Ala124 is a target for cathepsin D [59]. Created with BioRender.com.