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Fig. 8 | Translational Neurodegeneration

Fig. 8

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

Fig. 8

Molecular docking simulation of α-synuclein (α-syn) structures C4 (a) and C5 (b) bound to adenosine. 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. Adenosine only formed hydrogen bonds and hydrophobic interactions with N-terminal amino acid residues in C5 α-syn structure. In addition, adenosine also formed hydrogen bonds with amino acid residues within the N-terminus and NAC region in C4 α-syn structure. 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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