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Non-covalent microarrays from synthetic amino-terminating glycans—implications in expanding glycan microarray diversity and platform comparison

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Weishaupt,  Markus W.
Peter H. Seeberger - Automated Systems, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Seeberger,  Peter H.
Peter H. Seeberger - Automated Systems, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Citation

Li, C., Palma, A. S., Zhang, P., Zhang, Y., Gao, C., Silva, L. M., et al. (2021). Non-covalent microarrays from synthetic amino-terminating glycans—implications in expanding glycan microarray diversity and platform comparison. Glycobiology, cwab037. doi:10.1093/glycob/cwab037.


Cite as: http://hdl.handle.net/21.11116/0000-0008-8509-8
Abstract
Glycan microarrays have played important roles in detection and specificity assignment of glycan-recognition by proteins. However, the size and diversity of glycan libraries in current microarray systems are small compared to estimated glycomes, and these may lead to missed detection or incomplete assignment. For microarray construction, covalent and non-covalent immobilization are the two types of methods used, but a direct comparison of results from the two platforms is required. Here we develop a chemical strategy to prepare lipid-linked probes from both naturally-derived aldehyde-terminating and synthetic amino-terminating glycans that addresses the two aspects: expansion of sequence-defined glycan libraries and comparison of the two platforms. We demonstrate the specific recognition by plant and mammalian lectins, carbohydrate-binding modules and antibodies, and the overall similarities from the two platforms. Our results provide new knowledge on unique glycan-binding specificities for the immune-receptor Dectin-1 towards β-glucans and the interaction of rotavirus P[19] adhesive protein with mucin O-glycan cores.