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Fig. 9 | Translational Neurodegeneration

Fig. 9

From: Adenosine A1 receptor ligands bind to α-synuclein: implications for α-synuclein misfolding and α-synucleinopathy in Parkinson’s disease

Fig. 9

Molecular docking simulation of α-synuclein (α-syn) structures C2 (a), C5 (b), and C8 (c) bound to CPA; C2 (d), C5 (e), and C8 (f) bound to 2-aminoindan. Below full 3D representations show the magnified binding pocket of α-syn and the amino acid residue locations responsible for each drug binding. Bold black dashed lines and amino acid residues indicate hydrogen bonding, whereas the grey dashed lines and amino acid residues indicate hydrophobic interactions. Both CPA and 2-aminoindan formed hydrogen bonds and hydrophobic interactions with the N-terminal amino acids only (C5 and C8 α-syn structures) (b-c and ef, respectively). CPA also forms hydrogen bond and hydrophobic interactions with amino acids within the N-terminal and the NAC region (C2 α-syn structure) (a). In contrast, 2-aminoindan only forms hydrophobic interactions with the N-terminus and NAC domain in C2 α-syn structure (d). The molecular docking study was carried out using Autodock Vina module implemented in PyRx tool. Protein and ligand interactions were analyzed and visualized through Pymol and LigPlot + 

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