Abstract:The interaction between bovine serum albumin (BSA) and umbelliferone, an active component of Chinese herbs, with or without metal ions was investigated using fluorescence spectroscopy (FS) and UV.The experimental results showed that the umbelliferone molecules inserted into the hydrophobic pockets of BSA and quenched the intrinsic fluorescence of BSA by forming umbelliferone-BSA complex.The mechanism of fluorescence quenching was confirmed combining by both static quenching and nonradiative energy transferring.It was discovered that the apparent association constant (KA) increases in the presence of Cu2+ and Zn2+, whereas the spatial-distance (r) between umbelliferone molecule and fluorescent amino acid residues of the BSA and the binding sites (n) of umbelliferone molecules on BSA have no obviously change.Binding of umbelliferone molecules to BSA was a spontaneous supramolecular interaction in which entropy increased and Gibbs free energy decreaed.The interaction of the umbelliferone-BSA was driven mainly by electrostatic force which was enhanced by Cu2+ and Zn2+, thus the contribution of ΔH to ΔG increased in the presence of metal ions.
Key words:Active component of Chinese herbs;Umbelliferone;Bovine serum albumin;Metal ion;Fluorescence spectroscopy
刘雪锋,夏咏梅,方 云*,邹 鲁,刘玲玲 . 有/无金属离子Cu2+或Zn2+参与时中药有效成分伞形花内酯与生物大分子BSA的相互作用[J]. 光谱学与光谱分析, 2005, 25(08): 1301-1305.
LIU Xue-feng, XIA Yong-mei, FANG Yun*, ZOU Lu, LIU Ling-ling. Interaction between Bovine Serum Albumin and Umbelliferone with/without Metal Ions of Cu2+ or Zn2+. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2005, 25(08): 1301-1305.
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