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Shisheng Sun

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Supervisor of Master's Candidates  

Paper Publications

2. Shisheng Sun, Ganglong Yang, Ting Wang, Qinzhe Wang, Chao Chen, Zheng Li*. Isolation of N-linked glycopeptides by hydrazine-functionalized magnetic particles. Analytical and Bioanalytical Chemistry. 2010, 396(8): 3071-3078.

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DOI number:10.1007/s00216-010-3513-2.

Abstract:We introduce a novel combination of magnetic particles with hydrazine chemistry, dubbed as hydrazine-functionalized magnetic particles (HFMP) for isolation of glycopeptides. Four methods have been developed and compared for the production of HFMP by hydrazine modification of the surface of the carboxyl and epoxy-silanized magnetic particles, respectively. The evaluation of the capability and specificity of HFMP as well as the optimization of the coupling condition for capturing of glycoproteins were systematically investigated. The results showed that HFMP prepared by adipic dihydrazide functionalization from carboxyl-silanized magnetic particles (HFCA) displayed the maximum capture capacity and isolated efficiency for glycoprotein. When measured with glycoproteins, the capacity of the HFCA (1 g) for coupling bovine fetuin was 130 +/- 5.3 mg. The capability of this method was also confirmed by successful isolation of all formerly glycosylated peptides from standard glycoproteins and identification of their glycosylation sites, which demonstrated the feasibility of the HFCA as an alternative solid support for isolation of glycoproteins/glycopeptides.

Indexed by:Journal paper

Discipline:Natural Science

First-Level Discipline:Biology

Document Type:J

Translation or Not:no

Date of Publication:2010-02-19

Included Journals:SCI

Pre One:3. Wentian Chen, Shisheng Sun, Zheng Li*. Two Glycosylation Sites in H5N1 Influenza Virus Hemagglutinin That Affect Binding Preference by Computer-Based Analysis. PLOS One, 2011. 7(6): e38794.

Next One:1. Xiuxuan Sun, Yang Ganglong, Shisheng Sun, Rui Quan, Weiwei Dai, Bin Li, Chao Chen, Zheng Li*. The Hydroxyl-fuctionalized magnetic particles for purification of glycan-binding protein. Current Pharmaceutical Biotechnology. 2009, 10(8): 753-760.