The binding features of a series of 5-lipoxygenase (5-LOX) inhibitors (caffeic acid, NDGA,
AA-861, CDC, esculetin, gossypol and phenidone) to human 5-LOX have been studied by
using surface plasmon resonance biosensor (SPR) technology based Biacore 3000 and
molecular docking simulation analyses. The SPR results showed that the equilibrium
dissociation constant (KD) values evaluated by Biacore 3000 for the inhibitors showed a
good correlation with its reported IC50, suggesting that SPR technology might be applicable
as a direct assay method in screening new 5-LOX inhibitors at an early stage.
In addition, the 3D structural model of 5-LOX was generated according to the crystal
structure of rabbit reticulocyte 15-lipoxygenase, and the molecular docking simulation
analyses revealed that the predicted binding free energies for the inhibitors correlated
well with the KD values measured by SPR assay, which implies the correctness of the
constructed 3D structural model of 5-LOX. This current work has potential for application
in structure-based 5-LOX inhibitor discovery.