Add time:08/08/2019         Source:sciencedirect.com

In this study, the interaction between C.I. Acid Orange 7 (AO7) and human serum albumin (HSA) was firstly investigated using nuclear magnetic resonance (NMR) spectroscopy in combination with fluorescence quenching spectroscopy, three-dimensional fluorescence spectroscopy, UV–vis absorption spectroscopy, Fourier transform infrared (FT-IR) spectroscopy, circular dichroism (CD) spectroscopy and molecular modeling method in vitro. The results of NMR data confirmed that AO7 indeed interacted with HSA, and the hydrophobic portion of AO7 should be embedded to the hydrophobic pocket of HSA. The fluorescence quenching analysis revealed that AO7 can bind to HSA. The conformational change of HSA in the presence of AO7 was confirmed by synchronous fluorescence, three-dimensional fluorescence, UV–vis absorption, FT-IR and CD spectra. The binding distance between AO7 and tryptophan residue of HSA was calculated by the efficiency of fluorescence resonance energy transfer. Molecular modeling showed that hydrophobic force and hydrogen bonds were the major interaction between AO7 and HSA.

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