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Chemically-blocked Antibody Microarray for Multiplexed High-throughput Profiling of Specific Protein Glycosylation in Complex Samples
Published on: May 4, 2012
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(Glycan Binding) Activity-Based Protein Profiling in Cells Enabled by Mass Spectrometry-Based Proteomics.
Zak Vilen1,2, Abigail E Reeves1,2, Mia L Huang1,2
1Skaggs Graduate School of Chemical and Biological Sciences, Scripps Research, 10550 N. Torrey Pines Rd., La Jolla, CA 92037, USA.
Israel Journal of Chemistry
|May 3, 2023
Summary
Glycan modifications regulate cell functions but are complex to study. New glycan-binding probes and mass spectrometry techniques help identify proteins with specific glycan patterns and binding capabilities.
Area of Science:
- Biochemistry
- Cell Biology
- Glycoscience
Background:
- Glycans are crucial for cell recognition and function.
- Glycosylation complexity leads to incomplete annotation of glycan-modified proteins and glycan-binding proteins.
- Activity-based protein profiling inspired the development of novel probes.
Purpose of the Study:
- To address challenges in annotating glycan modifications and binding proteins.
- To describe the utility of glycan-binding and glycan-based probes.
- To highlight advancements in glycoscience through probe integration with mass spectrometry.
Main Methods:
- Development of glycan-binding and glycan-based probes.
- Application of activity-based protein profiling principles.
- Integration of probes with high-resolution mass spectrometry.
Main Results:
- Probes enable the assignment of proteins with specific glycan modifications.
- Probes facilitate the identification of proteins that bind glycans.
- Combined approaches significantly advance glycoscience.
Conclusions:
- Glycan-binding probes are powerful tools for characterizing protein glycosylation.
- Mass spectrometry integration enhances the study of complex glycan-protein interactions.
- These advancements improve our understanding of cell recognition and function.
