Du Hongyan, Xiang Junfeng, Zhang Yazhou, Tang Yalin, Xu Guangzhi
Beijing National Laboratory for Molecular Sciences, State Key Laboratory for Structural Chemistry of Unstable and Stable Species, Center for Molecular Sciences, Institute of Chemistry, Chinese Academy of Sciences, Beijing 100080, China.
J Inorg Biochem. 2008 Jan;102(1):146-9. doi: 10.1016/j.jinorgbio.2007.07.030. Epub 2007 Aug 6.
The action mechanism of vanadocene dichloride, Cp2VCl2 (Cp=eta5-C5H5), has been investigated by interaction with human serum transferrin for its promising antitumor activities. Our results have shown that Cp2VCl2 binds to transferrin and form a new complex, and the calculated apparent association constant is 1.37 x 10(5)M(-1) from the fluorescence quenching. Simultaneously, the variation of the secondary structure of transferrin occurs, most probably due to the coordination of the amino residues of protein with VIV. It was evidenced that Cp is released free in solution after VIV binding to transferrin by 1H NMR measurements. These results have shown that Cp2VCl2 forms a complex with transferrin, which may provide a possible pathway in the transport and targeted delivery of the antitumor agent.
二氯茂钒（Cp2VCl2，Cp = η5-C5H5）因其具有前景的抗肿瘤活性，已通过与人血清转铁蛋白相互作用对其作用机制进行了研究。我们的结果表明，Cp2VCl2与转铁蛋白结合形成一种新的复合物，通过荧光猝灭计算得到的表观缔合常数为1.37×10(5)M(-1)。同时，转铁蛋白的二级结构发生变化，最有可能是由于蛋白质的氨基残基与四价钒配位所致。通过1H NMR测量证明，四价钒与转铁蛋白结合后，Cp在溶液中游离释放。这些结果表明，Cp2VCl2与转铁蛋白形成复合物，这可能为抗肿瘤药物的运输和靶向递送提供一条可能的途径。
