| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1231474 | Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy | 2013 | 5 Pages |
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.
Graphical abstractThe fluorescence emission spectra of MH-BSA system at excited 280 nmFigure optionsDownload full-size imageDownload 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.
