期刊
JOURNAL OF LUMINESCENCE
卷 132, 期 10, 页码 2719-2729出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jlumin.2012.05.032
关键词
Bovine serum albumin; Human serum albumin; Scopoletin; Fluorescence; Binding constants; Thermodynamic parameters
类别
资金
- Education Department of Sichuan Province [12ZA171]
The interactions of scopoletin to bovine serum albumin (BSA) and human serum albumin (HSA) have been investigated by spectroscopic methods. The fluorescence tests indicated that the formation mechanism of scopoletin-BSA/HSA complexes belonged to the static quenching. The displacement experiments suggested that scopoletin primarily bound to tryptophan residues of BSA/HSA within site! (subdomain IIA). The binding distance of scopoletin to BSA/HSA was 2.38/2.34 nm. The thermodynamic parameters (Delta G, Delta H and Delta S) calculated on the basis of different temperatures revealed that the binding of BSA-scopoletin was mainly depended on van der Waals interaction and hydrogen bond, and yet the binding of HSA-scopoletin was strongly relied on the hydrophobic interaction and electrostatic interaction. The results of synchronous fluorescence, 3D fluorescence, UV-vis absorption, and FT-IR spectra showed that the conformations of BSA and HSA altered with the addition of scopoletin. In addition, the effects of some common ions on the binding constants of scopoletin to proteins were also investigated. (C) 2012 Elsevier B.V. All rights reserved.
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