title: Combined spectroscopies and molecular docking approach to characterizing the binding interaction between lisinopril and bovine serum albumin.
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 × 10(4) 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 ΔG(0), ΔH(0) and ΔS(0) 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.
authors: College of Pharmaceutical Science, Zhejiang University of Technology, Hangzhou, 310032, China.
authors: Min
authors: M
authors: Jiang
authors: College of Pharmaceutical Science, Zhejiang University of Technology, Hangzhou, 310032, China.
authors: Chuan-Ren
authors: CR
authors: Huang
authors: College of Pharmaceutical Science, Zhejiang University of Technology, Hangzhou, 310032, China.
authors: Qi
authors: Q
authors: Wang
authors: College of Pharmaceutical Science, Zhejiang University of Technology, Hangzhou, 310032, China.
authors: Ying-Yao
authors: YY
authors: Zhu
authors: College of Pharmaceutical Science, Zhejiang University of Technology, Hangzhou, 310032, China.
authors: Jing
authors: J
authors: Wang
authors: College of Pharmaceutical Science, Zhejiang University of Technology, Hangzhou, 310032, China.
authors: Jun
authors: J
authors: Chen
authors: College of Pharmaceutical Science, Zhejiang University of Technology, Hangzhou, 310032, China.|State Key Laboratory Breeding Base of Green Chemistry Synthesis Technology, Zhejiang University of Technology, Hangzhou, 310032, China.
authors: Jie-Hua
authors: JH
authors: Shi
mesh_terms: D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D017706:Lisinopril / Q000737:chemistry*; D008968:Molecular Conformation; D062105:Molecular Docking Simulation; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013050:Spectrometry, Fluorescence; D017550:Spectroscopy, Fourier Transform Infrared
chemical_list: D012710:Serum Albumin, Bovine; D017706:Lisinopril
keywords: bovine serum albumin; interaction; lisinopril; molecular docking; multi-spectroscopies