Nonstatistical binding of a protein to clustered carbohydrates
Nonstatistical binding of a protein to clustered carbohydrates
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DOI：
10.1073/pnas.96.21.11782
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发表时间：
1999-10-12
影响因子：
11.1
通讯作者：
Kahne, D
中科院分区：
文献类型：
--
作者：
Horan, N;Yan, L;Kahne, D
碳水化合物衍生自组装单层（SAMs）被用作模型系统来解决涉及细胞表面碳水化合物-蛋白质相互作用的问题。在这里，我们研究了碳水化合物表面密度对蛋白质结合度的影响。我们发现紫荆凝集素的结合选择性从一种碳水化合物配体切换到另一种碳水化合物配体，当碳水化合物配体的表面密度从chi（糖）接近0.1-1.0时增加。在所研究的所有表面密度下，多价结合都是可能的；因此，选择性的改变不仅仅是由于达到了允许多价接触的临界密度。相反，在高表面密度下，二级相互作用促进了碳水化合物结合选择性的转换。这些发现可能对细胞表面碳水化合物的组成和密度的变化如何影响生物识别过程和调节途径具有启示意义。
Carbohydrate-derivatized self-assembled monolayers (SAMs) are used as a model system to address issues involving cell-surface carbohydrate-protein interactions. Here we examine the influence of carbohydrate surface density on protein-binding avidity. We show that the binding selectivity of Bauhinia purpurea lectin switches from one carbohydrate ligand to another as the surface density of the carbohydrate ligands increases from values of chi(sugar) approximate to 0.1-1.0. Polyvalent binding is possible at all surface densities investigated; hence, the switch in selectivity is not due simply to the achievement of a critical density that permits polyvalent contacts. Instead, secondary interactions at high surface densities promote a switch in carbohydrate-binding selectivity. These findings may have implications for how changes in the composition and the density of cell-surface carbohydrates influence biological recognition processes and regulatory pathways.