CS结构修饰及其与AA相互作用的空间位阻效应  

Structural modification of chondroitin sulfate and the spatial baffle effect of interaction with methylene blue

作　　者：高贵珍[1,2] 焦庆才[1] 陈雷[1] 丁一磊[1] 

机构地区：[1]南京大学生命科学学院药物生物技术国家重点实验室 [2]宿州学院生化分析实验室,江苏宿州234000

出　　处：《兰州大学学报（自然科学版）》2005年第5期42-47,共6页Journal of Lanzhou University(Natural Sciences)

基　　金：国家科技攻关资助项目(2002EB020962).

摘　　要：为从分子水平探讨硫酸化多糖与小分子相互作用机理,本文采用氯磺酸-吡啶法(Wolfrom法)对硫酸软骨素(CS)进行结构修饰,制得了不同硫取代度的CS样品.应用光谱法研究了天青A(AA)与CS相互作用的吸收光谱,考察了硫取代度对CS抗凝血活性及AA与CS相互作用的影响,应用建立的酸性多糖与生物探针相互作用数学模型,测得AA与不同硫取代度的CS最大结合数分别为151,215,211和204,认为AA与CS相互作用具有空间位阻效应.In order to understand the mechanism for the interaction between sulfate polysaccharides and small molecules under the molecular level, structural modification of chondroitin sulfate （CS） by Wolfrom, a series of chondroitin sulfate samples with different sulfated degree are prepared. The interaction of chondroitin sulfate and Azur A （AA） is studied by absorption spectra, and the influence of the sulfated degree on the interaction and interference unit of CS is investigated. With the mathematical model of the interaction between acidic polysaccharides and biological probes, the maximum biding numbers of Azur A with different CS samples have been obtained as 151,215, 211 and 204. We consider that the interaction between Azur A and chondroitin sulfate shows steric hindrance.

关 键 词：硫酸软骨素 天青A 硫酸化 光谱法 

分 类 号：Q539[生物学—生物化学]