L-cysteine functionalized straticulate C3N4 for the selective enrichment of glycopeptides

J Chromatogr A. 2020 Jan 11:1610:460545. doi: 10.1016/j.chroma.2019.460545. Epub 2019 Sep 16.

Abstract

The facile enrichment of glycopeptides or glycoproteins poses great challenges for glycoproteomic research. In this study, a novel hydrophilic material, named zwitterionic hydrophilic L-cysteine derivatized straticulate-C3N4 composites (LCAC), were synthesized and evaluated for the enrichment of N-glycopeptides. LCAC exhibited good biocompatibility, excellent hydrophilicity and selectivity, by virtue of the large surface of C3N4 and the zwitterionic property offered by cysteine. LCAC demonstrated excellent performance for N-glycopeptide enrichment with the sensitivity of 0.033 fmol/µL, selectivity of 1:100, and high recovery rate (∼85%). The performance of LCAC was demonstrated by the identification of 35 N-glycopeptides from IgG, as well as capturing 1809 human urine N-glycopeptides corresponding to 876 N-glycoproteins. Comparing the LCAC with our developed phenylboronic acid functionalized material showed a certain complementary due to the different binding mechanism. The simple production and enhanced hydrophilic properties make the material a promising choice for glycoproteomics researches.

Keywords: Carbon nitride; Glycoproteome; Hydrophilic interaction chromatography; Mass spectrometry; Urine.

MeSH terms

  • Chromatography, Affinity
  • Cysteine / chemistry*
  • Glycopeptides / isolation & purification*
  • Glycopeptides / urine
  • Glycoproteins / isolation & purification*
  • Glycoproteins / urine
  • Humans
  • Hydrophobic and Hydrophilic Interactions
  • Nitriles / chemistry*
  • Sensitivity and Specificity

Substances

  • Glycopeptides
  • Glycoproteins
  • Nitriles
  • cyanogen
  • Cysteine