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采用荧光光谱和三维荧光光谱法研究了橙皮素(HSP)与牛血清白蛋白(BSA)之间的相互作用,并考察了共存金属离子Cu2+,Zn2+对二者相互作用的影响。实验结果表明,HSP对BSA的内源性荧光具有猝灭作用,猝灭类型为静态猝灭,作用力类型是氢键和范德华力,Cu2+,Zn2+的加入未改变HSP对BSA的猝灭类型和作用力类型。通过比较猝灭常数、结合常数、结合位点数、猝灭效率和三维荧光光谱图变化,推知Cu2+,Zn2+能与BSA产生结合作用,使其成为受制状态下的刚性肽链,从而影响HSP进入BSA疏水腔,减弱了HSP与BSA的结合能力,表现为与HSP存在竞争作用。
The interaction between hesperetin (HSP) and bovine serum albumin (BSA) was studied by fluorescence spectroscopy and three-dimensional fluorescence spectroscopy. The effects of coexistent metal ions Cu2 + and Zn2 + on their interaction were also investigated. The experimental results showed that HSP quenched the endogenous fluorescence of BSA, the quenching type was quiescent quenching, the type of force was hydrogen bond and van der Waal’s force, the addition of Cu2 + and Zn2 + did not change the quenching type and Force type. By comparing the quenching constants, binding constants, binding sites, quenching efficiency and changes of three-dimensional fluorescence spectra, we deduced that Cu2 + and Zn2 + can bind BSA and make it a rigid peptide chain in the controlled state, thus affecting the entry of HSP into BSA Hydrophobic cavity, weakened the binding capacity of HSP and BSA, showed a competitive effect with HSP.