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Fig. 7 | Translational Neurodegeneration

Fig. 7

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

Fig. 7

Molecular docking simulation of α-synuclein (α-syn) structures C1 (a), C4 (b), C5 (c) and C8 (d) bound to 1-aminoindan. Below full 3D representations show the magnified binding domains of α-syn and the amino acid residues in both the N- and C- termini of α-syn that facilitate drug binding. Bold black dashed lines and amino acid residues indicate hydrogen bonding, whereas the grey dashed lines indicate hydrophobic interactions. Hydrogen bonding of 1-aminoindan with C-terminal amino acid residues is observed in C1, C4, C5 and C8 α-syn structures. In addition, hydrophobic interactions occur between 1-aminoindan and N-terminal amino acid residues (C1 and C4 α-syn structures) and also between 1-aminoindan and portions of the NAC region (C5 and C8 α-syn structures). 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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Translational Neurodegeneration

ISSN: 2047-9158

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