Study of Interaction between Human Serum Albumin and Miconazole Nitrate Using Multi-Spectroscopic Methods

Abstract

The interaction of human serum albumin (HSA) and miconazole nitrate (MIN) had been studied by multi-spectroscopic methods. The inner filter effect was corrected before used the original data. The results indicated that MIN induced the fluorescence quenching of HSA was static quenching procedure. According to the Van’t Hoff equation, the interaction of HSA and MIN was determined by negative enthalpy change and positive entropy change, which showed that electrostatic forces were the major force in the binding process. The displacement experiments revealed that MIN binds in the vicinity of site I of HSA. The binding distance between Trp214 of HSA and MIN was 3.82 nm. Furthermore, the alternations of HSA secondary structure were calculated by FT-IR spectra. Upon formation of HSA-MIN complexes, the amount of α-helix structure reduced from 43.28% to 29.92%, β-sheet reduced from 22.59% to 18.79%, β-turn increased from 20.33% to 30.11% and random increased from 13.80% to 21.19%.