کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1409724 | 1501829 | 2011 | 6 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Study on the interaction between dihydromyricetin and bovine serum albumin by spectroscopic techniques Study on the interaction between dihydromyricetin and bovine serum albumin by spectroscopic techniques](/preview/png/1409724.png)
The interaction between dihydromyricetin (DMY) and bovine serum albumin (BSA) was investigated using fluorescence and ultraviolet spectroscopy at different temperatures under imitated physiological conditions. The experimental results revealed that dynamic quenching, static quenching and non-radiation energy transfer led to the fluorescence quenching. The obtained binding constants, binding sites and corresponding thermodynamic parameters at different temperatures indicate that hydrophobic forces play a major role in the interaction of DMY with BSA. According to Förster non-radiation energy transfer theory, the binding distance between BSA and DMY was found to be 3.26 nm. Synchronous fluorescence spectroscopy and FT-IR spectra showed the conformation of BSA changed in the presence of DMY. In addition, the effect of some common metal ions Cu2+, Ca2+, Mg2+, and Zn2+ on the binding constant between DMY and BSA was examined.
Journal: Journal of Molecular Structure - Volume 985, Issues 2–3, 31 January 2011, Pages 407–412