Fluorescence study on the interaction of human serum albumin with loureirin B. Issue 5 (2010)

• Record Type: Journal Article
• Authors: Chen, Xu; Ma, Jia-Ming; Yong, Ke-Lan; Lv, Jing-Ci; Zhang, Xia-Bing
• Is Part Of: Spectroscopy. Volume 24:Issue 5(2010)
• Page Start: 547
• Page End: 557
• Publication Date: 2010
• DOI: 10.3233/SPE-2010-0476
• Languages: English
• ISSNs: 0712-4813

Abstract

Abstract : 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 ) 2.68×10 4, 3.30×10 4 and 4.10×10 4 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.