期刊
TETRAHEDRON
卷 66, 期 29, 页码 5305-5310出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.tet.2010.05.038
关键词
Glycodendrimers; Dendrimers; Surface plasmon resonance; Inhibition binding assay; Multivalency
资金
- NIH [RO1 GM62444]
Understanding protein/carbohydrate interactions is essential for elucidating biological pathways and cellular mechanisms but is often difficult due to the prevalence of multivalent interactions. Here, we evaluate the multivalent glycodendrimer framework as a means to describe the inhibition potency of multivalent mannose-functionalized dendrimers using surface plasmon resonance (SPR). Using highly robust, mannose-functionalized dithiol self-assembled monolayers on gold surfaces, we found that glycodendrimers were efficient inhibitors of protein/carbohydrate interactions. IC50 values ranging from 260 nM to 13 nM were obtained for mannose-functionalized dendrimers with Concanavalin A. (C) 2010 Elsevier Ltd. All rights reserved.
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