Structure Analysis for Glycoprotein

What Are Glycoproteins Made of?

What Are Glycoproteins Made of?

Glycoproteins are composed of proteins that are covalently linked to carbohydrate chains (also known as glycans). These glycans are essential for the glycoprotein's stability, function, and interactions with other molecules. The carbohydrates attached to the protein backbone are highly variable, consisting of different sugar molecules such as glucose, galactose, mannose, and sialic acid, which can be linked in various configurations to form complex sugar structures. Glycoproteins play an indispensable role in numerous biological processes, including immune responses, cell signaling, and the regulation of protein stability. However, due to the complexity of their structure—comprising both proteins and carbohydrate chains—the analysis of glycoproteins presents significant challenges. These challenges arise from the heterogeneity of glycans, their low abundance in some biological systems, and the wide variety of structural modifications.

As a pioneering leader in the field, Creative Biolabs has leveraged its expertise and cutting-edge technologies to develop comprehensive glycoprotein structure analysis services. Our services are tailored to meet the needs of researchers, pharmaceutical companies, and biotechnology firms focused on glycoprotein structural characterization. By utilizing a wide range of glycoprotein analysis techniques, we help researchers uncover the intricacies of glycoprotein structure, improving their understanding of glycoprotein functional properties. With several years of experience, we take pride in offering innovative and highly reliable glycoprotein analysis solutions, ensuring our clients achieve success in their projects.

Fig.1 Schematic representation of methods for targeted and global enrichment of glycoproteins and glycopeptides.¹

Techniques for Glycoprotein Structure Analysis

To unravel the complexity of glycoprotein structures, a range of advanced techniques is used. These glycoprotein analysis techniques allow scientists to determine the exact structure of glycoproteins, including identifying the glycosylation sites and understanding how these modifications affect protein functionality.

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Applications of Glycoprotein Structure Analysis

Clinical Therapeutic Proteins

Glycoproteins in therapeutic proteins, such as monoclonal antibodies (mAbs), growth factors, and cytokines, are critical for the success of biopharmaceuticals. The glycosylation of therapeutic proteins can impact their pharmacokinetics, efficacy, and immune response. Detailed glycoprotein structure analysis is essential for optimizing the design of recombinant therapeutic glycoproteins and ensuring their clinical success. Our glycoprotein structure analysis in biopharmaceuticals helps ensure that therapeutic proteins have the correct glycosylation patterns for maximum safety and efficacy.

Serum Proteins

Serum glycoproteins, such as erythropoietin (EPO) and α-1-acid glycoprotein (AGP), are important biomarkers in disease diagnosis and therapeutic monitoring. By analyzing the glycosylation patterns of serum proteins, researchers can detect glycosylation changes associated with disease states, providing important insights for personalized medicine. Through our serum glycoprofiling services, we help identify glycosylation changes that are crucial for clinical diagnostics.

Viral Spike Proteins

Viral glycoproteins, particularly the spike proteins, are key to viral entry into host cells. The glycosylation patterns of viral glycoproteins influence their infectivity and ability to evade the host immune response. By studying these glycoproteins, researchers can gain critical insights into viral pathogenesis and the development of targeted therapies. Creative Biolabs offers glycosylation analysis services for virus glycoproteins, supporting the study of glycoproteins involved in SARS-CoV-2, HIV, and influenza.

Glycoproteins in Disease Treatment

Glycoproteins are often implicated in the pathogenesis of diseases such as cancer, Alzheimer's, and autoimmune disorders. Understanding the role of glycoproteins in disease through structure analysis is essential for identifying new biomarkers and therapeutic targets. Our customized glycoprotein analysis services support the identification of glycoproteins in disease treatment, enabling the development of novel therapies.

Vaccine Development

The glycosylation of viral glycoproteins has a significant impact on immune response and vaccine efficacy. By analyzing these glycoproteins' structure, researchers can enhance the design of vaccines and improve their effectiveness. Our glycosylation analysis services for COVID-19 glycoproteins help optimize the glycan profile of viral proteins, facilitating the development of more effective vaccines.

Glycoprotein Structure Analysis Services Facilitating Your Research

Using a combination of cutting-edge glycoprotein analysis technologies, we offer a full range of services, including glycan profiling, glycomic profiling, glycosylation site mapping, and glycan sequencing. Our tailored solutions are designed to meet the specific needs of your research with high precision.

Glycan Profiling

Glycan profiling is an innovative technique that focuses on quickly and efficiently capturing essential details about target glycans, rather than spending unnecessary time on intricate structural analysis. By using methods like capillary electrophoresis, liquid chromatography-electrospray ionization-mass spectrometry (LC-ESI-MS), high-performance liquid chromatography (HPLC), reversed-phase-high performance liquid chromatography (RP-HPLC), and the emerging lectin microarray, we can profile glycans in a fast, sensitive, and high-throughput way.

Glycomic Profiling

Glycomic profiling can identify a wide range of N- and O-glycans in biological samples, including secretions, cell lines, tissues, and organs. This method uses high-sensitivity mass spectrometric (MS) techniques such as electrospray ionization (ESI) and matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF MS), along with gas chromatography-mass spectrometry (GC-MS) linkage analysis, to capture detailed information on glycan structures and their roles in biological processes.

Glycosylation Site Mapping

Mapping glycosylation sites provides valuable insight into how glycans affect protein function and structure. It can also reveal key aspects of glycoprotein activity, microheterogeneity, and its potential impact on biological outcomes. Matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF MS) is widely used to map glycosylation sites across glycoproteins from various sources, such as plasma, cells, tissues, and whole organisms.

Glycan Sequencing

Glycan sequencing involves carefully releasing N- and O-glycans from glycopeptides using enzymatic or chemical methods, followed by solid-phase extraction and derivatization. This approach offers a detailed look at glycan sequences and structures, providing the essential data needed to understand their biological functions and contributions to cellular processes.

Glycoprotein structure analysis has become a regular study in glycosylation engineering, which is beneficial for the assignment of distinct functional properties to defined structural features. With decades of experience, Creative Biolabs has successfully completed a lot of therapeutic glycoprotein projects. We can offer a whole set of glycoprotein structure analysis services to help you get landmark development. We can also customize our offering to meet your specific project needs. If you are interested, please contact us without hesitation.

Published data

Glycoprotein structure analysis is essential for viral research. This study employs single-particle cryo-electron microscopy to capture the high-resolution (3.9 Å) structure of the post-fusion S2 subunit of the SARS-CoV spike glycoprotein. The results reveal significant conformational changes that occur in the S2 subunit during membrane fusion, particularly the formation of the HR1-HR2 six-helix bundle and the strong binding of the linker region. These changes are critical for the membrane fusion process. Furthermore, the findings provide crucial insights into how coronaviruses fuse with host membranes, which is essential for understanding viral entry. Additionally, the study identifies potential targets for developing broad-spectrum vaccines and therapies aimed at combating SARS-like coronaviruses. By utilizing single-particle cryo-EM, this research not only demonstrates the power of this technique in analyzing complex glycoprotein structures but also underscores its importance as an invaluable tool for advancing virology studies.

Fig.2 Structural changes of the SARS-CoV glycoprotein from pre-fusion to post-fusion detected by cryo-EM.²

FAQs

Q1: What is the purpose of glycoprotein structure analysis?

Glycoprotein structure analysis helps to uncover the detailed architecture of glycoproteins, including their glycan components. This is crucial for understanding their biological functions, interactions, and roles in diseases, and is particularly important for optimizing therapeutic proteins, vaccine development, and diagnostic tools.

Q2: What are the applications of glycoprotein structure analysis in viral research?

In viral research, glycoprotein analysis helps to examine viral spike proteins, which are key for viral entry into host cells. By studying their glycosylation patterns, researchers can gain insights into viral pathogenesis, immune evasion mechanisms, and design targeted therapies or vaccines. (Glycosylation Analysis Services for Virus Glyoprotein)

Q3: Which techniques are used to analyze glycoprotein structures?

Various advanced techniques are used, such as mass spectrometric (MS), lectin microarray, liquid chromatography-electrospray ionization-mass spectrometry (LC-ESI-MS), and cryo-EM. These methods enable high-resolution analysis of glycan compositions, glycosylation sites, and the impact of these modifications on protein function.

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Reference

1. Nilsson, Jonas, et al. "Targeting the glycoproteome." Glycoconjugate journal 30 (2013): 119-136. Distributed under Open Access license CC BY 2.0, without modification.
2. Fan, Xiaoyi, et al. "Cryo-EM analysis of the post-fusion structure of the SARS-CoV spike glycoprotein." Nature communications 11.1 (2020): 3618. Distributed under Open Access license CC BY 4.0, without modification.

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