4.6 Article

Boronic Acid Functionalized Core-Satellite Composite Nanoparticles for Advanced Enrichment of Glycopeptides and Glycoproteins

Journal

CHEMISTRY-A EUROPEAN JOURNAL
Volume 15, Issue 39, Pages 10158-10166

Publisher

WILEY-V C H VERLAG GMBH
DOI: 10.1002/chem.200901347

Keywords

enrichment; glycopeptides; glycoproteins; mass spectrometry; nanoparticles

Funding

  1. National Science and Technology [200703914100, 2006AA02Z134, 2009CBS25607, 2006AA02A30S]
  2. National Natural Science Foundation of China [20735005, 20875016, 30672394, 30530040]
  3. Ph D Programs
  4. Foundation of the Ministry of Eduction of China [200802460011]
  5. NCET
  6. Shanghai Projects [08DZ2293601]
  7. Shu Guang [B109]

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A core-satellite-structured composite material has been successfully synthesized for capturing glycosylated peptides or proteins. This novel hybrid material is composed of a silica-coated ferrite core and numerous satellites of gold nanoparticles with lots of anchors. The anchor 3-amino-phenylboronic acid. designed for cap luring target molecules, is highly specific toward glycosylated specie. The long organic chains bridging the gold surface and the anchors could reduce the steric hindrance among the bound molecules and suppress nonspecific bindings. Due to the excellent structure of the current material, the trap-and-release enrichment of glycosylated samples is quite simple, specific. and effective Indeed, the composite nanoparticles could be used for enriching glycosylated peptides and proteins with very low concentrations. and the enriched samples can be easily separated from bulk solution by it magnet. By using this strategy. the recovery of glycopeptides and glycoproteins after enrichment were found to be 55.9 and 71.6% separately, whereas the adsorption capacity of the composite nanoparticles was proven to be more than 79 mg, of glycoproteins per gram of the material. Moreover, the new composite nanoparticles were applied to enrich glycosylated proteins from human colorectal cancer tissues for identification of N-glycosylation sites. In all. 194 unique glycosylation sites mapped to 155 different glycoproteins have been identified. of which 165 sites (85.1%) were newly identified.

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