通过N端琥珀酰化辅助酶促去糖基化从肽N端释放N-聚糖。
Releasing N-glycan from peptide N-terminus by N-terminal succinylation assisted enzymatic deglycosylation.
作者信息
Weng Yejing, Sui Zhigang, Jiang Hao, Shan Yichu, Chen Lingfan, Zhang Shen, Zhang Lihua, Zhang Yukui
机构信息
1] Key Lab of Separation Sciences for Analytical Chemistry, National Chromatographic R. &A. Center, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, China [2] University of Chinese Academy of Sciences, Beijing 100049, China.
Key Lab of Separation Sciences for Analytical Chemistry, National Chromatographic R. &A. Center, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, China.
出版信息
Sci Rep. 2015 Apr 22;5:9770. doi: 10.1038/srep09770.
Due to the important roles of N-glycoproteins in various biological processes, the global N-glycoproteome analysis has been paid much attention. However, by current strategies for N-glycoproteome profiling, peptides with glycosylated Asn at N-terminus (PGANs), generated by protease digestion, could hardly be identified, due to the poor deglycosylation capacity by enzymes. However, theoretically, PGANs occupy 10% of N-glycopeptides in the typical tryptic digests. Therefore, in this study, we developed a novel strategy to identify PGANs by releasing N-glycans through the N-terminal site-selective succinylation assisted enzymatic deglycosylation. The obtained PGANs information is beneficial to not only achieve the deep coverage analysis of glycoproteomes, but also discover the new biological functions of such modification.
由于N-糖蛋白在各种生物过程中发挥着重要作用，全球范围内的N-糖蛋白组分析备受关注。然而，采用当前的N-糖蛋白组分析策略时，蛋白酶消化产生的N端糖基化天冬酰胺肽段（PGANs）因酶的去糖基化能力较差而难以被鉴定。然而，从理论上讲，在典型的胰蛋白酶消化物中，PGANs占N-糖肽的10%。因此，在本研究中，我们开发了一种新策略，通过N端位点选择性琥珀酰化辅助酶促去糖基化释放N-聚糖来鉴定PGANs。所获得的PGANs信息不仅有利于实现糖蛋白组的深度覆盖分析，还有助于发现这种修饰的新生物学功能。
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