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Combined spectroscopies and molecular docking approach to characterizing the binding interaction between lisinopril and bovine serum albumin
Author(s) -
Jiang Min,
Huang Chuanren,
Wang Qi,
Zhu Yingyao,
Wang Jing,
Chen Jun,
Shi Jiehua
Publication year - 2016
Publication title -
luminescence
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.428
H-Index - 45
eISSN - 1522-7243
pISSN - 1522-7235
DOI - 10.1002/bio.2984
Subject(s) - lisinopril , chemistry , bovine serum albumin , circular dichroism , hydrogen bond , binding constant , fluorescence spectroscopy , binding site , fluorescence , stereochemistry , biochemistry , molecule , organic chemistry , angiotensin converting enzyme , biology , physics , quantum mechanics , blood pressure , endocrinology
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 Δ G 0 , Δ H 0 and Δ S 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. Copyright © 2015 John Wiley & Sons, Ltd.