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Releasing N-glycan from peptide N-terminus by N-terminal succinylation assisted enzymatic deglycosylation.

ABSTRACT: 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.

SUBMITTER: Weng Y

PROVIDER: S-EPMC4405948 | biostudies-literature | 2015 Apr

REPOSITORIES: biostudies-literature

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Releasing N-glycan from peptide N-terminus by N-terminal succinylation assisted enzymatic deglycosylation.

Weng Yejing Y Sui Zhigang Z Jiang Hao H Shan Yichu Y Chen Lingfan L Zhang Shen S Zhang Lihua L Zhang Yukui Y

Scientific reports 20150422

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 deve ...[more]

PMID: 25902405

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