期刊
出版社
ELSEVIER
DOI: 10.1016/j.jchromb.2021.123049
关键词
Glycopeptide enrichment; Electrostatic repulsion-hydrophilic interaction chromatography (ERLIC); Arginine; Mesoporous self-assembly; Tissue
资金
- Natural Science Foundation of Shanghai [19ZR1412000]
- Science and Technology Commission of Shanghai Municipality (STCSM) [20520712500]
- Fundamental Research Funds for the Central Universities [JKJ01211718]
A novel hydrophilic two-dimensional composite material was used to selectively enrich glycopeptides from biological samples, showing potential application in protein post-translational modification research.
Considering the importance of glycopeptides in the clinical diagnosis of cancer and some serious diseases, the identification of glycopeptides from complex biological samples has attracted considerable attention. Effective pre-enrichment before mass spectrometry analysis plays an important role. In this work, a kind of hydrophilic two-dimensional composites (denoted as GO@MPDA@Arg) based on mesoporous polydopamine-graphene oxide were used to selectively enrich glycopeptides in biological samples. The mesoporous polydopamine (MPDA) layer self-assembled with template Pluronic F127 provided more binding sites to load arginine, and bound arginine enhanced the hydrophilicity of the material. As a result, GO@MPDA@Arg composites exhibited excellent enrichment performance for glycopeptides, containing good selectivity (IgG digests : BSA digests = 1:50, molar ratio), low detection limit for IgG digests (10 fmol mu L-1), high loading capacity for IgG digests (200 mu g mg(-1)), and good size exclusion (IgG digests : IgG : BSA = 1:100:100, mass ratio). In addition, mouse brain tissue was selected as the actual biological sample to further study the enrichment effect of GO@MPDA@Arg composites. In three parallel experiments, a total of 401 glycopeptides belonging to 233 glycoproteins were enriched from 200 mu g digestion of mouse brain extract. The enrichment results demonstrate that GO@MPDA@Arg composites have application potential for glycopeptides enrichment in protein post-translational modification research.
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