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Updated: Feb 14, 2026

Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of GoldIII
Published on: August 31, 2018
Fluorescence spectroscopy of osthole binding to human serum albumin
Guang-De Yang1, Cong Li1, Ai-Guo Zeng1
1School of Medicine, Xi'an Jiaotong University, No. 76 Yanta Westroad, Shaanxi Province, Xi'an 710061, PR China.
Abstract:
The interaction of human serum albumin (HSA) with osthole was investigated by fluorescence spectroscopy. Osthole can quench the fluorescence of HSA and the quenching mechanism is a static process. The binding site number n and apparent binding constant K were measured at different temperatures. The thermodynamic parameters ΔH0, ΔG0 and ΔS0 were calculated at different temperatures. The results indicated that electrostatic forces played a major role in the interaction of osthole with HSA. Results of osthole synchronous fluorescence and UV absorption spectra showed that the microenvironment and conformation of HSA were changed.
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