Table 1. Aβ contact points with α-syn dimer during MD simulations.
| Contact | 0 ns | 0.1 ns | 0.5 ns | 1.0 ns | Interaction | ||
| Aβ residue | α-syn1 residue | α-syn2 residue | |||||
| GLU3* | LYS6* | 6.2 | 6.5 | 6.0 | 2.8 | Electrostatic | |
| PHE4* | ILE88* | 3.9 | 3.6 | Hydrophobic | |||
| ARG5 | ILE88 | 4.2 | 6.5 | Hydrophobic | |||
| ASP7 | THR92 | 2.8 | 6.9 | Hydrophobic | |||
| GLU11* | LYS97* | 2.8 | 2.8 | 4.8 | Electrostatic | ||
| VAL12* | LYS97* | 4.7 | 4.2 | 4.8 | Hydrophobic | ||
| VAL12* | VAL95* | 3.6 | 6.1 | 4.7 | Hydrophobic | ||
| VAL12* | ALA91* | 3.8 | 4.1 | Hydrophobic | |||
| HIS13 | LYS32 | 4.2 | 3.6 | 3.7 | Hbond | ||
| GLN15 | LYS97 | 4.6 | 2.8 | Hbond | |||
| GLN15 | GLU105 | 5.7 | 6.5 | 6.5 | Possible Hbond | ||
| LYS16* | ASP98* | 4.7 | 2.8 | 2.8 | 2.8 | Electrostatic | |
| LYS16* | GLU28* | 5.5 | Electrostatic | ||||
| LEU17 | LYS32 | 4.8 | 4.0 | 5.7 | 6.4 | Hydrophobic | |
| PHE19 | PHE4 | 4.7 | 4.6 | Hydrophobic | |||
| PHE19 | VAL3 | 5.4 | 4.0 | Hydrophobic | |||
| ILE31 | GLY25 | 5.3 | 4.4 | 6.3 | Hydrophobic | ||
| ILE31 | ALA29 | 5.4 | Hydrophobic | ||||
| ILE31 | THR22 | 6.8 | Hydrophobic | ||||
| ILE31 | LYS21 | 5.6 | 6.0 | Hydrophobic | |||
| ILE32 | VAL26 | 6.8 | 4.7 | 4.9 | Hydrophobic | ||
| ILE32 | THR22 | 4.1 | 4.0 | Hydrophobic | |||
| LEU34 | GLU28 | 3.8 | 4.1 | 4.4 | Hydrophobic | ||
| LEU34 | ALA29 | 3.8 | 4.4 | 4.5 | 4.1 | Hydrophobic | |
| GLU37 | ALA29 | 6.2 | 4.5 | 4.3 | Hydrophobic | ||
| GLU38 | ALA29 | 4.4 | Hydrophobic | ||||
| ALA42 | THR33 | 3.8 | Hydrophobic | ||||
*
Indicates residues located at the points predicted to be critical for stabilization of the Aβ-α-syn complexes on the membrane. These resides of Aβ were mutated for additional analysis of Aβ-α-syn interactions.