中文摘要：

利用荧光和圆二色光谱研究了长春新碱（VCR）与人血清白蛋白（HSA）之间的相互作用 。通过荧光猝灭测得在288，298和308K时，VCR与HSA的结合常数K分别为2 .14×104，1 .73×104和1 .35×104L·mol-1，表明VCR与HSA间具有较强的结合作用，属于静态猝灭 。计算出焓变（△H）为-17.38kJ·mol-1，熵变（△S）为22 .62J·mol-1·K-1，结合分子模型理论计算的结果，表明VCR与HSA相互作用时在色氨酸（Trp）214残基和VCR分子中吲哚基间作用力以疏水作用力为主，但在VCR和HSA分子间以静电引力为主 。圆二色光谱（CD）的数据表明相互作用后HSA的二级结构发生了改变：HSA的α-螺旋的含量从51 .7%下降到32 .9%，β-折叠的含量增加了9 .2% 。

英文摘要：

The interaction between vincristine （VCR） and human serum albumin （HSA） was investigated by fluorescence and circular dichroism （CD） spectra at 288, 298 and 308 K. With fluorescence quenching method, the binding constants K were determined to be 2.14× 10^4, 1.73× 10^4 and 1.35× 10^4 L·moL^-1 respectively, indicating that the binding of VCR to HSA was strong, and the quenching mechanism was a static quenching. Enthalpy change （AH） was calculated to be - 17.38 kJ·moL^-1 and entropy change （AS） was 22.62 J·mol^-1·K^-1. Taking into account the result of molecule modeling study, all these results indicated that the hydrophobic interaction played major roles between the tryptophan （214） residue of HSA and the indole moiety of VCR, but the electrostatic interaction mostly existed between the molecules of HSA and VCR in the binding process. The secondary structure of HSA was altered （CD data） with reductions of a-helices from 51.7% to 32.9%, but increases β-sheet by about 9.2% after VCR bound to HSA.