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运用UV-Vis光谱、荧光光谱、同步荧光光谱、FT-IR光谱等手段,研究了在模拟人体生理条件下,牛血清白蛋白(BSA)与磷钼酸的相互作用。UV-Vis光谱显示,加入磷钼酸后,BSA的紫外吸收降低且吸收峰红移,表明磷钼酸与BSA形成了复合物;荧光猝灭光谱显示磷钼酸对BSA有荧光猝灭作用,且其荧光猝灭机理符合静态机制,磷钼酸与BSA结合的结合常数为:Ks=2.539×104L·mol-1;探针实验表明磷钼酸与BSA在结合位点I发生结合;Fster偶极-偶极非辐射能量转移机理确定了磷钼酸在BSA中与第214位色氨酸残基之间的距离r=1.93nm;FT-IR光谱显示磷钼酸诱导BSA的二级结构发生了变化,α-螺旋含量降低。
The interaction between bovine serum albumin (BSA) and phosphomolybdic acid was studied under simulated human physiological conditions using UV-Vis spectroscopy, fluorescence spectroscopy, synchronous fluorescence spectroscopy and FT-IR spectroscopy. The results of UV-Vis spectroscopy showed that the addition of phosphomolybdic acid decreased the UV absorption of BSA and the red shift of absorption peak, indicating that phosphomolybdic acid formed a complex with BSA. Fluorescence quenching spectroscopy showed that phosphomolybdic acid had a fluorescence quenching effect on BSA, The fluorescence quenching mechanism was in accordance with the static mechanism. The binding constant of phosphomolybdic acid to BSA was Ks = 2.539 × 104L · mol-1. Probe experiments showed that phosphomolybdic acid bound to BSA at binding site I, ster dipole-dipole non-radiative energy transfer mechanism to determine the distance between phosphomolybdic acid and the 214th tryptophan residue in BSA r = 1.93nm; FT-IR spectra showed that phosphomolybdic acid induced BSA secondary Structure changes, α-helix content decreased.