| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1231782 | Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy | 2016 | 6 Pages |
•We explored human serum albumin with butein in liposome by spectroscopic methods.•The fluorescence quenching mechanism is static quenching.•The thermodynamic parameters were calculated.•The effect of Butein upon the conformation of human serum albumin was investigated.•The partition coefficient of Butein (Kp) in PC liposomes was calculated
The interaction of Butein with human serum albumin in L-egg lecithin phosphatidycholine (PC) liposome has been investigated by fluorescence and absorption spectroscopy. The results of the fluorescence measurement indicated that Butein effectively quenched the intrinsic fluorescence of HSA via static quenching. The Stern–Volmer plots in all the liposome solutions showed a positive deviation from the linearity. According to the thermodynamic parameters, the hydrophobic interactions appeared be the major interaction forces between Butein and HSA. The effect of Butein on the conformation of HSA was also investigated by the synchronous fluorescence under the same experimental conditions. In addition, the partition coefficient of the Butein in the PC liposomes was also determined by using the fluorescence quenching process. The obtained results can be of biological significance in pharmacology and clinical medicine.
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