Combined spectroscopies and molecular docking approach to characterizing the binding interaction between lisinopril and bovine serum albumin |
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Authors: | Min Jiang Chuan‐ren Huang Qi Wang Ying‐yao Zhu Jing Wang Jun Chen Jie‐hua Shi |
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Institution: | 1. College of Pharmaceutical Science, Zhejiang University of Technology, Hangzhou, China;2. State Key Laboratory Breeding Base of Green Chemistry Synthesis Technology, Zhejiang University of Technology, Hangzhou, China |
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Abstract: | To further understand the mode of action and pharmacokinetics of lisinopril, the binding interaction of lisinopril with bovine serum albumin (BSA) under imitated physiological conditions (pH 7.4) was investigated using fluorescence emission spectroscopy, synchronous fluorescence spectroscopy, Fourier transform infrared spectroscopy (FTIR), circular dichroism (CD) and molecular docking methods. The results showed that the fluorescence quenching of BSA near 338 nm resulted from the formation of a lisinopril–BSA complex. The number of binding sites (n) for lisinopril binding on subdomain IIIA (site II) of BSA and the binding constant were ~ 1 and 2.04 × 104 M–1, respectively, at 310 K. The binding of lisinopril to BSA induced a slight change in the conformation of BSA, which retained its α‐helical structure. However, the binding of lisinopril with BSA was spontaneous and the main interaction forces involved were van der Waal's force and hydrogen bonding interaction as shown by the negative values of ΔG0, ΔH0 and ΔS0 for the binding of lisinopril with BSA. It was concluded from the molecular docking results that the flexibility of lisinopril also played an important role in increasing the stability of the lisinopril–BSA complex. Copyright © 2015 John Wiley & Sons, Ltd. |
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Keywords: | lisinopril bovine serum albumin interaction multi‐spectroscopies molecular docking |
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