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Citation: DONG She-Ying, XUE Chun-Xia, HUANG Ting-Lin. Interaction between Atorvastatin Calciumand Bovine Serum Albumin[J]. Acta Physico-Chimica Sinica, ;2007, 23(10): 1520-1524. doi: 10.3866/PKU.WHXB20071007 shu

Interaction between Atorvastatin Calciumand Bovine Serum Albumin

1.
College of Sciences, Xi’an University of Architecture and Technology, Xi’an 710055, P. R.China; School of Environment and Municipal Engineering, Xi’an University of Architecture and Technology, Xi’an 710055, P. R.China

Received Date: 23 April 2007
Available Online: 3 September 2007

The interaction between atorvastatin calcium (AC) and bovine serum albumin (BSA) was investigated using electrochemical techniques in conjunction with spectroscopy. Both enhancement and abatement actions of BSA on the peak current of AC were discussed in low and high BSA concentration ranges. In pH 7.17 phosphate buffer solution, AC caused an irreversible reduction peak on mercury electrode. With the addition of BSA into the AC solution, the peak current of AC changed and peak potential shifted. The results of linear-sweep voltammetry showed that the molecule of BSA came into being the hydrophobic tiny section where hydrophobic aromatic-group in AC molecule was embedded through hydrophobic interaction when the concentration of BSA was in the range from 1.0×10^-7 to 2.0×10^-6 mol·L^-1. The binding equilibrium constant and binding ratio were calculated as 1.67×10⁵ and 1:1, respectively. Furthermore, the results of UV absorption spectra showed that the UV absorption peak of BSA could red-shift slightly in the presence of AC. The interaction between AC and BSA could result in the change of conformationof BSA. Thus, α-helix structure in BSA was also decreased. The results of IR spectroscopy showed that AC could interact with sulfur-containing and nitrogen-containing groups in BSA molecular.
- Atorvastatin calcium; Bovine serum albumin; Linear-sweep voltammetry; UV absorption spectroscopy; Fourier transforminfrared spectroscopy
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