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Updated: May 7, 2026
A Lectin HPLC Method to Enrich Selectively-glycosylated Peptides from Complex Biological Samples
Published on: October 1, 2009
Brush polymer modified and lectin immobilized core-shell microparticle for highly efficient glycoprotein/glycopeptide
Yiting Pan1, Haihong Bai, Cheng Ma
1School of Life Science and Technology, Beijing Institute of Technology, Beijing 100081, PR China; National Center for Protein Sciences Beijing, State Key Laboratory of Proteomics, Beijing Proteome Research Center, Beijing Institute of Radiation Medicine, Beijing 102206, PR China.
Researchers developed novel core-shell microparticles for improved lectin immobilization, enhancing glycoprotein analysis. This advancement aids in identifying biomarkers for diseases like cancer and diabetes.
Area of Science:
- Biochemistry
- Materials Science
- Analytical Chemistry
Background:
- Protein glycosylation is crucial for biological processes and implicated in diseases such as cancer, diabetes, and inflammation.
- Profiling protein glycosylation variations is vital for discovering diagnostic biomarkers and therapeutic targets.
- Enrichment of glycoproteins/glycopeptides is essential for mass spectrometry (MS) analysis due to low natural abundance.
Purpose of the Study:
- To develop an improved method for lectin immobilization to enhance glycoprotein and glycopeptide enrichment.
- To overcome limitations of conventional lectin immobilization techniques, including low surface area and poor lectin accessibility.
Main Methods:
- Synthesized core-shell microparticles with a silica core and a brush-like polymer shell using surface-initiated atom transfer radical polymerization (SI-ATRP).
- Immobilized lectins onto the flexible, brush-like polymer chains on the microparticle surface.
- Utilized the enhanced microparticles for affinity enrichment of glycoproteins/glycopeptides prior to MS analysis.
Main Results:
- The brush-like polymer shell provided a high surface area and flexible support for lectin immobilization, leading to high loading capacity.
- Improved accessibility of immobilized lectins was achieved compared to conventional methods.
- Successful enrichment of glycoproteins/glycopeptides was demonstrated, facilitating their identification.
Conclusions:
- Core-shell microparticles with brush-like polymer shells offer a superior platform for lectin immobilization.
- This novel approach significantly enhances glycoprotein/glycopeptide enrichment efficiency for MS-based analysis.
- The method holds promise for advancing biomarker discovery in various diseases.
