Abstract
For evaluating the weak interaction between sugar chains and proteins, regular glycol-array technology might not be effective because of the many washing steps between the binding and visualization of the bound proteins. It is crucial to eliminate the washing steps and to visualize the binding interaction at the real time. Using our original array-type sugar chain-immobilized chip (named array-type Sugar Chip, A-SC) and SPR imaging technology, an easy and conventional analytical method was developed for such a weak interaction. This method was applied to evaluate the sugar chain binding property of novel proteins, as well as of various viruses. Here, we focus on the glycosaminoglycan (GAG)-immobilized A-SC and report the results of analysis for the GAG structures to which human herpesviruses (HHVs) bind at the molecular level.
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Suda, Y., Zhang, X., Nakamura-Tsuruta, S., Sobel, M., Okuno, T., Wakao, M. (2015). Conventional and Easy Analysis of Virus-Binding GAG Structure Using Array-Type Sugar Chip. In: Taniguchi, N., Endo, T., Hart, G., Seeberger, P., Wong, CH. (eds) Glycoscience: Biology and Medicine. Springer, Tokyo. https://doi.org/10.1007/978-4-431-54841-6_14
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DOI: https://doi.org/10.1007/978-4-431-54841-6_14
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Publisher Name: Springer, Tokyo
Print ISBN: 978-4-431-54840-9
Online ISBN: 978-4-431-54841-6
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