Computational and experimental investigation of DNA repair protein photolyase interactions with low molecular weight drugs

Abstract

This paper reports the previously unknown interactions between eight low molecular weight commercially available drugs (130800Da) and DNA repair protein photolyase using computational docking simulations and surface plasmon resonance (SPR) experiments. Theoretical dissociation constants, Kd, obtained from molecular docking simulations were compared with the values found from SPR experiments. Among the eight drugs analyzed, computational and experimental values showed similar binding affinities between selected drug and protein pairs. We found no significant differences in binding interactions between pure and commercial forms of the drug lornoxicam and DNA photolyase. Among the eight drugs studied, prednisone, desloratadine, and azelastine exhibited the highest binding affinity (Kd=1.65, 2.05, and 8.47M, respectively) toward DNA photolyase. Results obtained in this study are promising for use in the prediction of unknown interactions of common drugs with specific proteins such as human clock protein cryptochrome. Copyright (c) 2013 John Wiley & Sons, Ltd.