Spectroscopic and molecular docking studies on the interaction betweenN-acetyl cysteine and bovine serum albumin
作者： Ali Jahanban-Esfahlan , Vahid Panahi-Azar , Sanaz Sajedi
DOI: 10.1002/BIP.22697
关键词:
摘要: The interaction between N-acetyl cysteine (NAC) and bovine serum albumin (BSA) was investigated by UV–vis, fluorescence spectroscopy, molecular docking methods. Fluorescence study at three different temperatures indicated that the intensity of BSA reduced upon addition NAC static quenching mechanism. Binding constant (Kb) number binding sites (n) were determined. for in order 103 M−1, obtained to be equal 1. Enthalpy (ΔH), entropy (ΔS), Gibb's free energy (ΔG) as thermodynamic values also achieved van't Hoff equation. Hydrogen bonding van der Waals force major intermolecular forces process it spontaneous. Finally, mode clarified using which good agreement with results spectroscopy experiments. © 2015 Wiley Periodicals, Inc. Biopolymers 103: 638–645, 2015.
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