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Issue 42, 2017
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Decoding glycan protein interactions by a new class of asymmetric N-glycans

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Abstract

N-Glycans are normally involved in crucial physiological and disease processes by interactions with glycan-binding proteins. So far structurally defined N-glycans have been good candidates for glycan binding study. Herein, a class of homogeneous asymmetric N-glycans was synthesized by coupling glycan-oxazoline and N-glycans using EndoM N175Q catalyzed quick glycan extension. Branch-biased binding and spacial inhibition caused by the bulky group on the other branch of N-glycan were observed in glycan protein interactions involving lectins and these glycans by glycan microarray study. These new compounds are valuable for functional glycomic studies to better understand new functions of glycans and glycan-binding proteins.

Graphical abstract: Decoding glycan protein interactions by a new class of asymmetric N-glycans

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Supplementary files

Article information


Submitted
14 Sep 2017
Accepted
10 Oct 2017
First published
10 Oct 2017

Org. Biomol. Chem., 2017,15, 8946-8951
Article type
Paper

Decoding glycan protein interactions by a new class of asymmetric N-glycans

Z. Wu, Y. Liu, L. Li, X. Wan, H. Zhu, Y. Guo, M. Wei, W. Guan and P. G. Wang, Org. Biomol. Chem., 2017, 15, 8946
DOI: 10.1039/C7OB02303K

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