喹啉修饰β-环糊精键合胆酸客体的热力学研究  

Binding thermodynamics of quinolinyl-modified β-cyclodextrins with bile salts

作　　者：李楠[1,2] 陈湧[1,2] 张瀛溟[1,2] 李志强[1,2] 刘育[1,2] 

机构地区：[1]元素有机化学国家重点实验室 [2]南开大学化学系,天津300071

出　　处：《中国科学：化学》2010年第9期1355-1362,共8页SCIENTIA SINICA Chimica

基　　金：国家重点基础研究发展计划重大研究计划(2006CB932900);国家自然科学基金(20932004,20721202&20772062)资助

摘　　要：采用微量热滴定、核磁共振和分子模拟等方法研究了三唑基喹啉修饰β-环糊精(1)和羟基喹啉基修饰β-环糊精(2)同胆酸(CA)、脱氧胆酸(DCA)、甘胆酸(GCA)和牛磺胆酸(TCA)的键合行为.二维核磁和分子模拟研究表明胆酸客体分子的尾链和D环部分从大口端进入了环糊精空腔.微量热滴定研究表明两种喹啉基修饰环糊精键合胆酸客体的过程由焓驱动,并且伴随着明显的熵损失,说明主-客体间键合的驱动力主要来自于氢键和范德华相互作用.与天然环糊精相比,喹啉基修饰环糊精对胆酸客体的键合有着更为有利的焓变和更为不利的熵变.The binding behaviors of two β-cyclodextrin derivatives bearing 8-hydroxyquinolino and triazolylquinolino groups with bile salts were studied in aqueous buffer solution （pH 7.20） by means of microcalorimetrical titration,2D NMR spectroscopy and molecular modeling.The results showed that the side chain and D-ring of bile salts were encapsulated in the β-CD cavity from the wide opening.Thermodynamically,the host-guest binding behaviors were mainly driven by the favorable enthalpic changes,accompanied by the unfavorable entropic changes,and the hydrogen-bonding interactions and van der Waals interactions were the main driven forces governing the host-guest binding.

关 键 词：环糊精 喹啉 胆酸 热力学 量热滴定 

分 类 号：O631.1[理学—高分子化学]