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Application of molecular modelling and spectroscopic approaches for investigating the binding of tanshinone IIA to human serum albumin
- Source :
-
Journal of Chemical Thermodynamics . Mar2013, Vol. 58, p206-210. 5p. - Publication Year :
- 2013
-
Abstract
- Abstract: The interaction of tanshinone IIA and human serum albumin (HSA) has been characterised by molecular modelling, fluorescence, Fourier transform infrared (FT-IR) and circular dichroism (CD) spectroscopic methods. The results of molecular modelling suggested that tanshinone IIA located within the binding pocket of subdomain IIA of HSA is held mainly by hydrophobic forces. Fluorescence titration revealed that tanshinone IIA could quench the intrinsic fluorescence of HSA. The binding constants at three temperatures (296, 303, and 310)K are (6.42·104, 1.54·105, and 4.35·105)dm3 ·mol−1, respectively. In addition, the studies of CD spectroscopy and FT-IR spectroscopy showed that the binding of tanshinone IIA to HSA changed molecular conformation of HSA. [Copyright &y& Elsevier]
Details
- Language :
- English
- ISSN :
- 00219614
- Volume :
- 58
- Database :
- Academic Search Index
- Journal :
- Journal of Chemical Thermodynamics
- Publication Type :
- Academic Journal
- Accession number :
- 85023453
- Full Text :
- https://doi.org/10.1016/j.jct.2012.11.009