草药物与人血白蛋白相互作用的分光光度法研究  

Study on Spectrophotometry of the Interaction Between Drug and Human Serum Albumin

作　　者：刘永和[1] 刘改云[2] 黄海燕[1] 

机构地区：[1]邵阳学院生物与化学工程系,湖南邵阳422000 [2]邵阳学院图书馆,湖南邵阳422000

出　　处：《邵阳学院学报（自然科学版）》2010年第1期53-56,共4页Journal of Shaoyang University：Natural Science Edition

基　　金：湖南省教育厅科研基金项目(06C744)资助

摘　　要：以曙红Y为光谱探针,采用分光光度法探讨抗癌药物足叶乙甙对人血白蛋白中曙红Y的竞争结合规律,研究足叶乙甙与人血白蛋白的相互作用及结合.结果表明,曙红Y与人血白蛋白以静电作用力为主进行结合,形成电子转移配合物.曙红Y与人血白蛋白结合后,药物足叶乙甙的加入对这种结合产生破坏,争夺并占据人血白蛋白的结合点位,使曙红Y从结合态变成游离态,同时生成新的更为稳定的结合体—人血白蛋白与药物足叶乙甙复合物,其结合比约为7.93molVp16/molHSA.由此说明:足叶乙甙不仅与人血白蛋白存在有效的结合点位,而且具有较好的结合强度和结合容量.这些既是足叶乙甙在人体内贮存和运输的条件,也是其产生抗癌活性的药理基础.This study attempts to investigate the antineoplastic （Vp16）＇ s competitive binding principle toward Eosin Y in Human Serum Albumin （HSA）, and explore the interaction between Etoposide and HAS as well as its binding ratio, by using Eosin Y as the spectroscopic probe. The result shows that Eosin Y and HSA were combined in the form of electrostatic interactions, to form the electron transfer complex. After the combination of Eosin Y and Human Serum Albumin, Drug Etoposide will destroy the combination to take up the combining point of HAS, which transforms Eosin Y from conjugated form into ionized form and meanwhile generates a more stable combination-complex of HSA and Drug Etoposide with a binding molar ratio of 7.93molVp16/molHSA. It thus reveals that the join point of VP16 and HAS is effective and the bonding strength and binding capacity are pretty good. They are not only the precondition of the storage and transport of Vp16 in the body, but also the pharmacological basis of its antitumor activity.

关 键 词：人血白蛋白 足叶乙甙 曙红Y 分光光度法 

分 类 号：R914[医药卫生—药物化学]