Multivalent interaction of cyclodextrin vesicles, carbohydrate guests, and lectins: a kinetic investigation.
Multivalent interaction of cyclodextrin vesicles, carbohydrate guests, and lectins: a kinetic investigation.
复制标题
DOI：
10.1021/la1038975
复制
发表时间：
2011-02
期刊：
影响因子：
--
通讯作者：
R. Vico;Jens Voskuhl;B. Ravoo
中科院分区：
文献类型：
--
作者：
R. Vico;Jens Voskuhl;B. Ravoo
当两亲性β-环糊精的单层双层囊泡通过主-客体相互作用与麦芽糖和乳糖-金刚烷偶联物修饰时，人造糖杯自组装。麦芽糖修饰的囊泡在凝集素刀豆蛋白A存在下聚集，而乳糖修饰的囊泡在凝集素花生凝集素存在下聚集。通过400 nm处随时间变化的光密度测量，研究了囊泡、碳水化合物和凝集素三元体系中存在的正交多价界面相互作用的动力学。用动态光散射法监测囊泡和囊泡集合体的平均尺寸。聚集过程被评估为凝集素浓度、囊泡浓度以及糖-金刚烷结合物对囊泡的表面覆盖率。囊泡聚集的初始速率与凝集素和环糊精囊泡浓度呈线性关系。此外，每种凝集素都需要囊泡表面碳水化合物的特征临界密度。这些观察结果可以预测三元超分子体系在其组分不同浓度下的响应。此外，可以准确地确定多价受体(例如多结合位点蛋白)中的有效结合位点分离。这种方法可以推广到其他配体-受体系统的界面上的多价非共价相互作用。
An artificial glycocalix self-assembles when unilamellar bilayer vesicles of amphiphilic β-cyclodextrins are decorated with maltose- and lactose-adamantane conjugates by host-guest interactions. The maltose-decorated vesicles aggregate in the presence of lectin concanavalin A whereas the lactose-decorated vesicles aggregate in the presence of lectin peanut agglutinin. The kinetics of the orthogonal multivalent interfacial interactions present in this ternary system of vesicles, carbohydrates, and lectins were studied by time-dependent measurements of the optical density at 400 nm. The average vesicle and vesicle aggregate sizes were monitored by dynamic light scattering. The aggregation process was evaluated as a function of lectin concentration, vesicle concentration, and surface coverage of the vesicles by the carbohydrate-adamantane conjugates. The initial rate of vesicle aggregation scales linearly with the lectin as well as the cyclodextrin vesicle concentration. Furthermore, each lectin requires a characteristic critical density of carbohydrates at the vesicle surface. These observations allow a prediction of the response of the ternary supramolecular system at different concentrations of its components. Also, the effective binding site separation in a multivalent receptor such as a multiple binding site protein can be accurately determined. This methodology can be extended to multivalent noncovalent interactions in other ligand-receptor systems at interfaces.