利福平与人血清白蛋白作用的荧光光谱

蛋白质是一类重要的生物大分子，它不仅是构成细胞内原生质的主要成分，也是生命现象的物质基础。对于蛋白质的探索是最复杂的课题之一。 以荧光光谱为手段，文章研究了药物利福平(Rifampicin capsules)与人血清白蛋白(HSA)的作用，测量发现利福平和人血清白蛋白的色氨酸残基的结合位置为R=2.567 nm, 临界距离R₀为2.433 nm。利福平-HSA的Lineweaver-Burk猝灭曲线的离解常数K_d=19.42×10-6 mol·L-1且结合常数K_s=5.149×104 L·mol-1。

Fluorescence Spectroscopy Study of Humen Serum Albumin Quenched by Rifampicin Capsules

It is obvious that the albumin is a kind of important large biophysical molecular. The albumin is the main component of plasma within cell. It is also the matter basis of life phenomenon. The fluorescence spectroscopy of humen serum albumin (HSA) and the interaction of HSA and the rifampicin capsules (lfp) were studied. When the rifampicin capsules (lfp) was added into HSA solution gradually, an interesting new phenomenon emerged in emission spectrum. The combination constant of rifampicin capsules (lfp) is about Ks = 5.149 x 10(4) L x mol(-1), and the dissociation constant is about Kd = 19.42 x 10(-6) mol x L(-1). The quenching process of rifampicin capsules (lfp)-HSA is not dynamic quenching, which resulted from the molecular diffusion and collision. That is the static quenching process resulting from the chemical component between molecules. The energy transfer efficiency between rifampicin capsules (lfp) and HSA is E=0.42. According to these calculation results, the combination position between the binding site of rifampicin capsules (lfp) and the tryptophane of HSA is about R=2.567 nm. The critical distance, when transfer efficiency equals 50%, is about R0 = 2.433 nm.