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Molecular spectroscopic on interaction between Methyl hesperidin and Buman serum albumin
- Source :
-
Spectrochimica Acta Part A: Molecular & Biomolecular Spectroscopy . Feb2013, Vol. 102, p200-204. 5p. - Publication Year :
- 2013
-
Abstract
- Abstract: The interaction of Methyl hesperidin (MH) with Buman serum albumin was studied by spectroscopic methods including Fluorescence quenching technology, UV absorbance spectra and Fourier transform infrared (FT-IR) spectroscopy under simulative physiological conditions. The result of fluorescence titration revealed that Methyl hesperidin could quench the intrinsic fluorescence of BSA and the quenching mechanism should be a combined quenching process. The binding constants at three temperatures (296, 303, and 310K) were 1.82, 2.69, and 3.4×104 Lmol−1, respectively. The distance between donor (BSA) and acceptor (MH) was 5.54nm according to the Förster theory of non-radiation energy transfer. In addition, FT-IR spectroscopy showed that the binding of MH to BSA changed the secondary structure of protein. [Copyright &y& Elsevier]
Details
- Language :
- English
- ISSN :
- 13861425
- Volume :
- 102
- Database :
- Academic Search Index
- Journal :
- Spectrochimica Acta Part A: Molecular & Biomolecular Spectroscopy
- Publication Type :
- Academic Journal
- Accession number :
- 84598466
- Full Text :
- https://doi.org/10.1016/j.saa.2012.10.012