Wolfenden Mark L, Cloninger Mary J
Department of Chemistry and Biochemistry and Center for Bioinspired Nanomaterials, Montana State University, 108 Gaines Hall, Bozeman, Montana 59717, USA.
J Am Chem Soc. 2005 Sep 7;127(35):12168-9. doi: 10.1021/ja053008n.
G4-, G5-, and G6-PAMAM dendrimers were functionalized with mixtures of mannose and glucose in varying ratios, and the relative affinities of these compounds for Concanavalin A (Con A) were evaluated using the hemagglutination assay. As the ratio of mannose to glucose increases, the relative activity in the hemagglutination assay (on a per sugar basis) increases linearly. Methyl mannose binds to Con A with an affinity 4-fold higher than that of methyl glucose; multivalency amplifies this trend. The mannose/glucose-functionalized dendrimer results reported here suggest that the affinity of multivalent associations can be attenuated in predictable, reliable ways based on monovalent affinities of the ligands.
将G4、G5和G6型聚酰胺-胺（PAMAM）树枝状大分子用不同比例的甘露糖和葡萄糖混合物进行功能化修饰，并使用血凝试验评估这些化合物对伴刀豆球蛋白A（Con A）的相对亲和力。随着甘露糖与葡萄糖比例的增加，血凝试验中的相对活性（以每个糖为基础）呈线性增加。甲基甘露糖与Con A的结合亲和力比甲基葡萄糖高4倍；多价性放大了这一趋势。此处报道的甘露糖/葡萄糖功能化树枝状大分子的结果表明，基于配体的单价亲和力，可以以可预测、可靠的方式减弱多价缔合的亲和力。
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