Fe^(3+)对V_(B_1)与牛血清白蛋白相互作用的影响

Effect of Fe^(3+) on the Interaction of V_(B_1) and Bovine Serum Albumin

采用荧光光谱法考察Fe^(3+)对V_(B_1)与牛血清白蛋白(BSA)相互作用的影响。试验结果表明,V_(B_1)对BSA的内源性荧光有猝灭作用,猝灭类型为动态猝灭,作用力类型为氢键和范德华力。Fe^(3+)的加入并未改变V_(B_1)对BSA的猝灭类型和作用力类型,但对其猝灭速率常数(k_q)、结合常数(K_A)以及结合位点数(n)会有不同程度的影响。同步荧光光谱显示V_(B_1)主要与BSA中的色氨酸残基作用,引起其构象或周围环境的改变。

The interaction of VB1 and bovine serum albumin （BSA） was studied in the presence of Fe 3＋by fluores-cence spectroscopy. The results indicated that V B1 could quench the intrinsic fluorescence of BSA, the quenching mechanism was static quenching and the main binding force was hydrogen bond and Vander Waals. The fluores-cence quenching mechanism and the main binding force were not changed in the presence of Fe 3＋, but the quenching rate constant（kq）,the binding constants（KA） and the binding sites（n） were changed in different de-grees. Synchronous spectra showed that VB1 binded to tryptophan residue and changed its microenvironment.