The molecular mechanism of galbanic acid (GBA) binding to matrix metalloproteinase 9 (MMP9) wasinvestigated by fluorescence quenching, absorption spectroscopy, FT-IR, molecular docking and molec-ular dynamics (MD) simulation procedures. The fluorescence emission of MMP9 was quenched by GBA.The titration of MMP9 by various amount of GBA was also followed by UV–Vis absorption spectroscopy.The results revealed that GBA, as a biologically active sesquiterpene coumarin derivative, has an abilityto bind strongly to MMP9.Molecular docking results indicated that the main active binding site for GBA has been located in ahydrophobic cavity in the vicinity of Zn atom. Moreover, MD simulation results suggested that GBA asa coumarin derivative can interact with MMP9, without affecting the secondary structure of MMP9. MDsimulations, molecular docking as computational methods from one hand and experimental data fromother hand reciprocally supported each other.
