Structure of Human Phosphodiesterase 5A1 Complexed with Avanafil Reveals Molecular Basis of Isoform Selectivity and Guidelines for Targeting Î±-Helix Backbone Oxygen by Halogen Bonding.

J Med Chem. 2020 Aug 13;63(15):8485-8494. doi:10.1021/acs.jmedchem.0c00853. Epub 2020 Jul 27

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Phosphodiesterase 5A1 (PDE5) is a key target for treating cardiovascular diseases and erectile dysfunction. Here, we report the crystal structure of PDE5 complexed with the sole second generation drug avanafil. Analysis of protein-drug interactions revealed the structural basis of avanafil's superior isoform selectivity. Moreover, a halogen bonding was observed between avanafil and a backbone carbonyl oxygen of an adjacent Î±-helix, whose contribution to inhibitory potency illustrates the feasibility of exploiting Î±-helix backbone in structure-based drug design.

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Structure of Human Phosphodiesterase 5A1 Complexed with Avanafil Reveals Molecular Basis of Isoform Selectivity and Guidelines for Targeting Î±-Helix Backbone Oxygen by Halogen Bonding.

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