27 February 2006 Dendrimer optimization for a glucose-sensitive fluorescent assay
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A fluorescent assay based on the competitive binding between glycosylated PAMAM dendrimer and glucose with the sugar-binding lectin Concanavalin A has been developed. This assay, composed of the glycodendrimer and Alexa Fluor 647 labeled Concanavalin A, has shown a large dynamic response to physiological concentrations of glucose. The larger dynamic range is believed to be due to the spheriodal shape of the dendrimer molecule, which eliminates the multiple binding of the same dextran chain to the Concanavalin A tetramer that plagued previous approaches. However, in order to further understand the operation of the assay and optimize the dynamic response, the dendrimer construction must be modified to determine the optimum degree of glycosylation. In this paper, a description of the assay function and the change in fluorescence response with various formulations of glycodendrimers are shown. Theories are also presented as means of understanding the various assay responses with different degrees of dendrimer functionalization.
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Hope T. Beier, Hope T. Beier, Bennett L. Ibey, Bennett L. Ibey, Rebecca M. Rounds, Rebecca M. Rounds, Michael V. Pishko, Michael V. Pishko, Gerard L. Coté, Gerard L. Coté, } "Dendrimer optimization for a glucose-sensitive fluorescent assay", Proc. SPIE 6094, Optical Diagnostics and Sensing VI, 60940I (27 February 2006); doi: 10.1117/12.645357; https://doi.org/10.1117/12.645357

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