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作 者:张攀 孙鹏飞 林铭昌 高振飞 陈国颂[1] ZHANG Pan;SUN Pengfei;LIN Mingchang;GAO Zhenfei;CHEN Guosong(Department of Macromolecular Science,Fudan University,Shanghai 200433,China;Institute of Advanced Materials,Nanjing University of Posts and Telecommunications,Nanjing 210023,China)
机构地区:[1]复旦大学高分子科学系,上海200433 [2]南京邮电大学材料科学与工程学院,南京210023
出 处:《高等学校化学学报》2019年第1期160-165,共6页Chemical Journal of Chinese Universities
基 金:国家自然科学基金(批准号:21504016)资助~~
摘 要:采用非共价键合胶束(NCCM)的组装策略,制备了表面为糖聚合物的纳米粒子,利用动态光散射技术,实时跟踪了在溶液中糖与蛋白相结合的动力学数据,并以聚集体形成的速度来体现不同的蛋白对相同组装体的结合能力强弱.实验结果表明,对表面覆盖100%乳糖的组装体,各蛋白的结合能力表现为SBA Lec A≈Galectin 3>ECA≈Galectin 1,表明蛋白的糖结合位点个数及其空间分布对多价作用的动力学有较大影响.基于此模型,对人半乳凝素-3与糖结合的方式进行了初步探究.Non-covalently connected micelles(NCCM)strategy was employed to obtain glyco-micelles covered by sugars in a convenient way.The impact factors for the recognition between carbohydrate and protein in solution were studied using dynamic light scattering(DLS)in real time.The results indicate that the agglutination ability of different lectins is of significant distinction,as measured by the formation rate of aggregates.For glyco-micelles covered by 100%lactose,the binding rates to different lectins can be recorded as SBA LecA≈Galectin 3>ECA≈Galectin 1,which suggests that not only number of binding sites but also how they are displayed have great influence on the kinetics of the multivalent interaction.Meanwhile,Human Galectin 3,a protein of important biological function with rather mysterious binding behavior,was studied further as an application of the method.
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