| Autor: |
Xu Chen, Jia-Ming Ma, Ke-Lan Yong, Jing-Ci Lv, Xia-Bing Zhang |
| Předmět: |
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| Zdroj: |
Spectroscopy: An International Journal; 2010, Vol. 24 Issue 5, p547-557, 11p, 1 Diagram, 1 Chart, 6 Graphs |
| Abstrakt: |
The interaction between loureirin B (Lour B) and human serum albumin (HSA) was investigated by fluorescence and UV–vis absorption spectroscopy. Experimental results indicated that loureirin B had a strong ability to quench the intrinsic fluorescence of HSA through a dynamic quenching procedure. The fluorescence quenching data revealed that the quenching constants (KSV) 2.68×104, 3.30×104 and 4.10×104 l/mol at 300, 310 and 320 K, respectively. Based on the thermodynamic parameters obtained, the positive values of enthalpy change ΔH and entropy change ΔS suggested that hydrophobic forces played a major role in the interaction of Lour B with HSA. According to Förster theory of energy transfer, the distance r between HSA and Lour B was calculated to be 2.85 nm. Furthermore, the effect of Lour B on the conformation of HSA was analyzed by synchronous fluorescence and three-dimensional fluorescence spectra. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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