Spectroscopic investigation on the food components-drug interaction: the influence of flavonoids on the affinity of nifedipine to human serum albumin.

Nifedipine (NDP) is used extensively for the clinical treatment of a number of cardiovascular diseases. Herein, the interaction between human serum albumin (HSA) and NDP and the influence of flavonoids, rutin and baicalin, on their binding properties were investigated in vitro by means of fluorescence and absorption spectroscopy. The fluorescence of HSA was quenched remarkably by NDP and the quenching mechanism was considered as static quenching by forming a complex. The results of thermodynamic parameters indicate that both hydrogen bonds and hydrophobic interactions play the main role in the binding process and the binding process was spontaneous. The binding distance between the amino acid residue of HSA and NDP is 2.608 nm, which indicates that the energy transfer from HSA to NDP can occur with high probability. The decreased association constants and the increased binding distance of NDP binding to HSA in the presence of flavonoids were both due to their competitive binding to the site I of HSA. The results obtained from synchronous fluorescence and three-dimensional fluorescence spectra showed that the interaction between HSA and NDP caused the conformational changes of HSA and the synergism effects of NDP and flavonoids induced the further conformational changes of HSA.