• 文献标题:   Hydrophilic arginine-functionalized mesoporous polydopamine-graphene oxide composites for glycopeptides analysis
  • 文献类型:   Article
  • 作  者:   ZHENG Y, PU CL, ZHAO HL, GU QY, ZHU TY, LAN MB
  • 作者关键词:   glycopeptide enrichment, electrostatic repulsionhydrophilic interaction chromatography erlic, arginine, mesoporous selfassembly, tissue
  • 出版物名称:   JOURNAL OF CHROMATOGRAPHY BANALYTICAL TECHNOLOGIES IN THE BIOMEDICAL LIFE SCIENCES
  • ISSN:   1570-0232 EI 1873-376X
  • 通讯作者地址:  
  • 被引频次:   2
  • DOI:   10.1016/j.jchromb.2021.123049 EA JAN 2022
  • 出版年:   2022

▎ 摘  要

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.