publication . Article . Other literature type . 2015

Interaction of NAC With BSA

Ali Jahanban-Esfahlan;
  • Published: 22 Aug 2015 Journal: Biopolymers, volume 103, pages 638-645 (issn: 0006-3525, Copyright policy)
  • Publisher: Wiley
The interaction between N-acetyl cysteine (NAC) and bovine serum albumin (BSA) was investigated by UV–vis, fluorescence spectroscopy, and molecular docking methods. Fluorescence study at three different temperatures indicated that the fluorescence intensity of BSA was reduced upon the addition of NAC by the static quenching mechanism. Binding constant (Kb) and the number of binding sites (n) were determined. The binding constant for the interaction of NAC and BSA was in the order of 103 M−1, and the number of binding sites was obtained to be equal to 1. Enthalpy (ΔH), entropy (ΔS), and Gibb's free energy (ΔG) as thermodynamic values were also achieved by van't H...
free text keywords: Biophysics, Organic Chemistry, Biochemistry, Biomaterials, General Medicine
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