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The Investigation of the Interaction between Daidzin and Bovine Serum Albumin by Fluorescence Spectroscopy
Ist Teil von
Applied Mechanics and Materials, 2014-10, Vol.664 (Mechatronics and Mechanical Engineering I), p.402-409
Ort / Verlag
Zurich: Trans Tech Publications Ltd
Erscheinungsjahr
2014
Link zum Volltext
Quelle
Alma/SFX Local Collection
Beschreibungen/Notizen
We investigated the mutual interaction of daidzin with bovine serum albumin (BSA) by fluorescence spectroscopy. The results revealed that daidzin cause the fluorescence quenching of BSA through a static quenching procedure. The Stern-Volmer quenching constant (Ksv) were calculated at different temperature. The binding site (n), apparent binding constant (Ka) and corresponding thermodynamic parameters △Go, △Ho, △So were calculated and the van der Waals interaction, hydrogen bonds and hydrophobic interactions play an important role in stabilizing the complex. Besides, we also studied the effect of Cu2+, Ni2+, Mn2+ and Co2+ on the binding constants between daidzin and BSA, it is shows that the binding of BSA and daidzin is strengthened in the presence metal ions.