کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1231474 | 1495266 | 2013 | 5 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Molecular spectroscopic on interaction between Methyl hesperidin and Buman serum albumin Molecular spectroscopic on interaction between Methyl hesperidin and Buman serum albumin](/preview/png/1231474.png)
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 310 K) were 1.82, 2.69, and 3.4 × 104 L mol−1, respectively. The distance between donor (BSA) and acceptor (MH) was 5.54 nm 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.
The fluorescence emission spectra of MH-BSA system at excited 280 nmFigure optionsDownload as PowerPoint slideHighlights
► Multi-spectroscopy techniques were associated to study the interactions between MH and BSA.
► The quenching mechanism of fluorescence was a combined quenching process.
► The binding constants were calculated.
► The change of the BSA secondary structure induced by MH binding was measured by FT-IR spectroscopic methods.
► These results are important for clinical pharmacology.
Journal: Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy - Volume 102, February 2013, Pages 200–204