中文摘要：

研究了单取代酞菁锌（1-[4-（2-羧基乙基）苯氧基]酞菁锌,即ZnPcC1）与白蛋白（人血清白蛋白HSA和牛血清白蛋白BSA）的共价和非共价结合作用,进而研究了结合方式对ZnPcC1的光谱性质和存在状态的影响。结果表明,ZnPcC1可以通过成酰胺键的方式与白蛋白构成共价结合物（摩尔组成比大约为7∶1）;ZnPcC1与白蛋白之间存在较强的非共价相互作用,结合常数大约为1.0×105mol-1.L。结合位点竞争实验表明,非共价相互作用的结合位点位于人血清白蛋白的亚域ⅠB。ZnPcC1与白蛋白结合后,无论是共价结合还是非共价结合,均展现出比游离酞菁更明显的单体特征吸收,这是一个有利于光动力治疗的性质。共价结合导致ZnPcC1的单体特征吸收峰红移约5 nm,而非共价结合则没有导致红移。

英文摘要：

Interaction between 1-[4-（2-carboxyl-ethyl-）phenoxy] phthalocyanine Zinc（Ⅱ）（ZnPcC1） and albumin（human serum albumin or bovine serum albumin） was studied.ZnPcC1 can be covalently bound to albumin through amide bond formation.The molar ratios of ZnPcC1 to albumins are found to be about 7∶1 in the covalent bioconjugates.On the other hand,there are strong non-covalent interactions between ZnPcC1 and albumins with a binding constant of ca.1.0×105 mol-1·L.Binding sites competition experiments suggest that the binding site locates in subdomain ⅠB of human serum albumin.When conjugated to albumin,no matter covalent conjugation or non-covalent conjugation,the ZnPcC1 exhibit more distinctive characteristic monomer absorption than the free ZnPcC1,which is a property beneficial to photodynamic therapy.Covalent conjugation results in the Q-band of ZnPcC1 red-shifting about 5 nm,whereas non-covalent conjugation does not lead to red-shift.