The effect of the structural differences in the reducing terminus of sugars on the binding affinity of carbohydrates and proteins analyzed using photoaffinity labeling.
The effect of the structural differences in the reducing terminus of sugars on the binding affinity of carbohydrates and proteins analyzed using photoaffinity labeling.
复制标题
使用光亲和标记分析糖还原末端的结构差异对碳水化合物和蛋白质结合亲和力的影响。
DOI:
10.1016/j.bmc.2010.11.067
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发表时间:
2011
期刊:
影响因子:
--
通讯作者:
Akiyo Sakushima
中科院分区:
文献类型:
--
作者:
Isao Ohtsuka;Yutaka Sadakane;Mari Higuchi;Noriyasu Hada;Junko Hada;Nobuko Kakiuchi;Akiyo Sakushima
Because carbohydrates and proteins bind with such low affinity, the nature of their interactions is not clear. Photoaffinity labeling with diazirin groups is useful for elucidating the roles of carbohydrates in these binding processes. However, when carbohydrate probes are synthesized according to this conventional method, the reducing terminus of the sugar is opened to provide an acyclic structure. Because greater elucidation of carbohydrate–protein interactions requires a closed-ring carbohydrate in addition to the photoreactive group, we synthesized new molecular tools. The carbohydrate ligands were synthesized in three steps (glycosylation with allyl alcohol, deprotection, and ozonolysis). Specific binding proteins for carbohydrate ligands were obtained by photoaffinity labeling. Closed ring-type carbohydrate ligands, in which the reducing sugar is closed, bound to lectins more strongly than open ring-type sugars. Carbohydrate to protein binding was observed using AFM.