对溴苯甲醛-4-苯基-2-噻唑脲与人血清蛋白相互作用的研究

The Interaction Between (E)-2-(2-(4-bromobenzylidene)hydrazinyl)-4-phenylthiazole and Albumin Human

采用荧光法研究了对溴苯甲醛-4-苯基-2-噻唑脲(BHP)与人血清蛋白(HSA)之间的相互作用。根据溴苯甲醛-4-苯基-2-噻唑脲与HSA相互作用的荧光敏华作用,利用Stern-Volmer方程及非辐射能量转移理论处理试验数据,采用同步荧光光谱探讨了BHP对HSA构象的影响。结果表明,BHP可以使HSA的荧光增强,表明两者之间发生了能量转移,能量转移的机理是BHP与HSA结合形成了复合物。荧光增强(敏化)效应主要源于给体-受体间的偶极-偶极作用的能量转移。能量转移的结果为内原发色基团(给体donor)的荧光被猝灭和外源发色基团(受体acceptor)荧光被敏化,计算得到其敏化常数为-2.494 5×104。同步荧光光谱表明,相互作用引起HSA构象变化,提示结合位点更接近于色氨酸。

To study the interaction between（E）-2-（2-（4-bromobenzylidene）hydrazinyl）-4-phenylthiazole（BHP） and Albumin Human by fluorescence,the Stern-Volmer curve and theory of non-radiation energy transfer was used to deal with the dates of fluorescence quench.The synchronous spectrum was used to investigate the conformational changes of HSA.Results showed that BHP enhanced the fluorescence of HSA.The mechanism of energy transfer was that BHP formed complexes with HSA.Fluorescence enhancement（sensitization effect） stemed mainly from the donor-the dipole-dipole effect between receptor and energy transfer.Fluorescence of the primary base group（to the body donor） was quenched and that of exogenous basement regiment receptors（acceptor） was sensitized.The sensitization constant was-2.494 5 ×104.Synchronous fluorescence spectra showed that the interaction caused change of HSA conformation,prompting binding sites closer to tryptophan.