Chemical informatics uncovers a new role for moexipril as a novel inhibitor of cAMP phosphodiesterase-4 (PDE4).

Though moexipril's similarity to even the closest known PDE4 inhibitor was modest – a Tanimoto coefficient of 0.35 qualifies it as close to a scaffold-hop for the ECFP4 fingerprints [Ref.: PMID 18416545 ] – over the entire PDE4 ligand set its expectation value ( E -value), at 1.71 −11 , was highly significant compared to the random background. 3.2 Models of moexipril bound to catalytic domain of PDE4 As the structure of the PDE4 core catalytic domain is well defined by X-ray crystallography, with numerous co-crystal structures available for a range of inhibitors from different structural classes, we additionally undertook the molecular docking of moexipril to consider its potential as a PDE4 inhibitor.

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