Figure 1. Structural characteristics of α-Syn monomers and fibril aggregates. (A) α-Syn is composed of three different regions: a positively charged amphiphilic N-terminus (residues 1-60), a hydrophobic nonamyloid (NAC) region (residues 61-95), and a negatively charged CTD (residues 96-140); they may have different functions. (B) The secondary structure of α-Syn. (C) The structure of the amino acid residues of α-Syn. (D) The fibril structure (secondary structure) of α-Syn. (E) The fibril structure (amino acid residues) of α-Syn. All the structure diagrams are from the PDB database (https://www.rcsb.org/), and the corresponding colors are marked.