Glycoprotein Structure Analysis
Glycoproteins are widely used in biomedicine, but their complex structure and heterogeneity can be obstacles in research. We have developed a structure analysis platform with multiple world-leading technologies to help customers comprehensively progress in glycoprotein research. CD BioGlyco has the confidence to be your essential research assistant in the field of glycobiology.
Overview of Glycoprotein Structure Analysis
Glycosylation is one of the most common protein post-translational modifications. It usually determines the folding and transport of proteins, and regulates almost all extracellular activities, including cell-to-cell communication and cell-matrix interactions. It has been shown that specific glycosylation changes are the key to disease progression and can have diagnostic value for multiple disease types, such as cancer and inflammation. Therefore, glycoproteins can be used as effective biomarkers for disease detection and targets for drug and vaccine development. Although glycoproteins are important, the complex structure of carbohydrates and their derivatives in biological samples makes the global analysis of glycoproteins extremely challenging.
In recent years, mass spectrometry (MS) has become a powerful tool for glycoprotein analysis. The microarray platform has also become an indispensable tool for characterizing glycan structures and studying glycosylation-related biological interactions. Although the emergence of mass spectrometry-based proteomics research provides huge opportunities for the analysis of glycoproteins, the low abundance of many glycoproteins and the heterogeneity of glycans greatly increase the technical difficulty, which requires very professional research personnel and extremely sophisticated analytical instruments. In order to overcome these obstacles, more methods have been developed in recent years, which have contributed to the comprehensive analysis of glycoproteins.
Core Technologies for Glycoprotein Characterization
CD BioGlyco leverages state-of-the-art technologies to deliver unparalleled accuracy and resolution in glycoprotein structure analysis. Our core technologies include advanced MS techniques, such as electrospray ionization mass spectrometry (ESI-MS) and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS), for precise mass measurement and glycan profiling. We also employ high-performance liquid chromatography (HPLC) and ultra-high-performance liquid chromatography (UHPLC) for efficient glycan separation and quantification. Complementing these, our nuclear magnetic resonance (NMR) spectroscopy capabilities provide atomic-level structural details of isolated glycans and glycosylation sites.
Unveiling Glycoprotein Structures with CD BioGlyco
- N-linked Glycan Analysis: We offer detailed characterization services for glycans linked to asparagine residues, including the identification of high mannose, complex, and heterogeneous glycans.
- O-linked Glycan Analysis: We offer specialized parsing services for glycans linked to serine or threonine residues, which are essential for understanding mucins and other highly glycosylated proteins.
- Glycosylation Site Mapping: Our lab offers precise identification of specific amino acid residues linked by glycan chains, providing key insights into the biological function of glycoproteins.
- Glycan Linkage Analysis: Our company offers specific glycosidic bond linkage analysis between monosaccharide units, which is essential for understanding the three-dimensional structure and recognition properties of glycans.
- Monosaccharide Composition Analysis: We provide monosaccharide fractions within glycans for precise quantitative analysis, providing clients with essential building block information.
- Quantitative Glycan Profiling: We provide precise relative and absolute quantification of glycan species in different samples or experimental conditions to enable comparisons.
SARS-CoV-2 Glycosylation Profiling
CD BioGlyco combines multiple technology platforms to provide clients with accurate SARS-CoV-2 glycosylation analysis to accelerate the development of vaccines and other therapeutic agents. Our services include the comprehensive characterization of N-linked and O-linked glycosylation sites of SARS-CoV-2 spike proteins, as well as the quantitative analysis of glycosylation structures.
Workflow
Applications
- Our services can be used to deepen the understanding of biological processes involving glycosylation, such as cell-cell communication, host-pathogen interactions, and protein folding.
- Our services are essential for characterization, quality control, and comparability studies of glycoproteins, including monoclonal antibodies, fusion proteins, and vaccines.
- Our services can be used to identify new glycoprotein biomarkers for use in disease-related conditions, particularly in oncology, inflammatory diseases, and neurodegenerative disorders.
Advantages of Us
- We pride ourselves on unparalleled analytical depth, providing not just identification but also detailed structural elucidation of even the most complex glycan modifications.
- Our high-resolution instrumentation ensures accurate mass measurements and comprehensive fragmentation data, critical for unambiguous structural assignments.
- Our team comprises experienced glycobiology experts who interpret complex data with scientific rigor, translating raw analytical outputs into meaningful biological insights.
Publication Data
Technology: MS, MS/MS
Journal: Analytical Chemistry
Published: 2023
IF: 6.7
Results: This literature provides insights into the use of MS for structure-specific N-glycoproteomics analysis, particularly the qualitative and quantitative analysis of isomeric glycopeptide structures. By synthesizing stable isotope-labeled N-glycopeptide standards, combined with collision energy modulation, the study reveals the possible rearrangement of monosaccharide units or the breakage of mannose cores in collision chambers, resulting in the generation of “Ghost” fragment ions, which leads to misassignment of glycan structures. In addition, the study describes for the first time the rearrangement phenomenon of salivary acids under collision energy, which provides a new perspective for the accurate identification of specific glycan structures in human samples. The researchers effectively prevented false-positive structure identification in glycoproteomics analysis by setting a minimum intensity threshold for fragment ions. These findings represent a critical step toward improving the accuracy and reliability of glycoproteomics measurements.
Fig.1 MS/MS spectra of G2FS IgG glycopeptides at different collision energies. (Campos, et al., 2023)
Frequently Asked Questions
CD BioGlyco provides comprehensive glycoprotein structure analysis services to help with customers' in-depth study of the heterogeneity and function of glycoproteins. Our professional research teams are proud to provide customers with different types of analysis data according to their specific needs. If you are interested in our services, please contact us to obtain more information.
Associated Services
Beyond our core glycoprotein structure analysis, CD BioGlyco offers a range of complementary services to support your comprehensive glycobiology research and development needs. These services are designed to provide a holistic understanding of your samples and facilitate your project's success.
Reference
- Campos, D.; et al. "Ghost" fragment ions in structure and site-specific glycoproteomics analysis. Analytical Chemistry. 2023, 95(27): 10145-10148. (Open Access)
