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. Author manuscript; available in PMC: 2024 Aug 3.
Published in final edited form as: Cell. 2023 Jul 7;186(16):3350–3367.e19. doi: 10.1016/j.cell.2023.06.004

Figure 6. Interactions between F0502B and α-Syn fibril.

Figure 6.

(A) π-π stacking among F0502B molecules. The distance between neighboring aromatic rings of F0502B is ~3.7 Å. Detailed interaction distances are labeled.

(B) Summary of the molecular interactions between F0502B (orange) and α-Syn fibril (black). Polar interactions (blue dashed lines) and non-dipolar interactions (red spiked arcs) are depicted with interaction distances.

(C) T-shaped π-π interactions between F0502B and Tyr39 residues in three consecutive α-Syn molecules (i, i+1, i+2) along the fibril. Detailed interaction distances and the dihedral angles formed by π planes are labeled.

(D) Cation-anion-π-π network between the phenol head of F0502B and α-Syn residues Lys80, Glu46, and Tyr39. Detailed interaction distances are labeled.

(E) Hydrogen bonding and halogen bonding interactions between the phenol head of F0502B and α-Syn. The phenolic hydroxyl group of F0502B forms hydrogen bonds with the backbone amide of Gly41. The bromine of F0502B interacts with the sidechain hydroxyl group of Thr44 via halogen bonding. Detailed interaction distances are labeled.

(F) Hydrophobic and halogen bonding interactions between the tail of F0502B and α-Syn. The methyl group of F0502B forms hydrophobic interactions with Val82. The fluorine of F0502B forms halogen bonding interactions with Glu83. Detailed interaction distances are labeled.

See also Figure S6.