Wu Zhigang, Liu Yunpeng, Li Lei, Wan Xiu-Feng, Zhu He, Guo Yuxi, Wei Mohui, Guan Wanyi, Wang Peng George
Department of Chemistry and Center of Diagnostics & Therapeutics, Georgia State University, Atlanta, GA 30303, USA.
Org Biomol Chem. 2017 Oct 31;15(42):8946-8951. doi: 10.1039/c7ob02303k.
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.
N-聚糖通常通过与聚糖结合蛋白相互作用参与关键的生理和疾病过程。到目前为止，结构明确的N-聚糖一直是聚糖结合研究的良好候选物。在此，通过使用EndoM N175Q催化的快速聚糖延伸反应，将聚糖恶唑啉与N-聚糖偶联，合成了一类均一的不对称N-聚糖。通过聚糖微阵列研究，在涉及凝集素和这些聚糖的聚糖-蛋白质相互作用中，观察到N-聚糖另一分支上的庞大基团引起的分支偏向性结合和空间抑制。这些新化合物对于功能糖组学研究具有重要价值，有助于更好地理解聚糖和聚糖结合蛋白的新功能。
