Complexes between C.I. Acid Orange 6 and human serum albumin, a multi-spectroscopic approach to investigate the binding behavior

Add time:08/03/2019    Source:sciencedirect.com

The interaction mechanism of Acid Orange 6 (AO6) with human serum albumin (HSA) was investigated firstly by using fluorescence quenching technique, UV absorbance, circular dichroism (CD), Fourier transform infrared (FT-IR), three-dimensional fluorescence spectroscopy in combination with molecular modeling method under simulative physiological conditions. Fluorescence data indicated that there is a single class of binding sites between AO6 and HSA, and the alterations of HSA secondary structure in the presence of AO6 was confirmed by synchronous fluorescence, UV, CD, FT-IR and three-dimensional fluorescence spectra. The efficiency of fluorescence resonance energy transfer provided the binding distance (r) of 2.83 nm for AO6–HSA system. Furthermore, the thermodynamic parameters enthalpy change (ΔH0) and entropy change (ΔS0) for the reaction were calculated to be −5.77 kJ mol−1 and 109.42 J mol−1 K−1, respectively, according to Van't Hoff equation, these data suggested that both hydrophobic forces and hydrogen bonding play a major role in the binding of AO6 to HSA, which agrees well with the results of molecular modeling study. Experimental results showed that the interaction between AO6 and HSA induced a conformational change of HSA, which was proved by the qualitative and quantitative analysis data of different spectroscopic techniques under simulative physiological conditions.

► Utilized multi-spectroscopy technique and molecular modeling method. ► Investigated the interaction between AO6 and HSA qualitatively and quantitatively. ► The intrinsic fluorescence of HSA was quenched through dynamic quenching mechanism. ► The addition of AO6 can induce the conformational changes of HSA. ► Both hydrophobic forces and hydrogen bonding play a major role in the interaction.

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