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Related Concept Videos

Protein Glycosylation01:25

Protein Glycosylation

Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
Chemistry of Carbohydrates03:25

Chemistry of Carbohydrates

Carbohydrates are an essential part of the diet in humans and animals. Grains, fruits, and vegetables are natural sources of carbohydrates that provide energy to the body, particularly through glucose, a simple sugar that is a component of starch and an ingredient in many staple foods. The stoichiometric formula (CH2O)n, where n is the number of carbons in the molecule represents carbohydrates. In other words, the ratio of carbon to hydrogen to oxygen is 1:2:1 in carbohydrate molecules. This...
Chemistry of Carbohydrates03:25

Chemistry of Carbohydrates

Carbohydrates are an essential part of the diet in humans and animals. Grains, fruits, and vegetables are natural sources of carbohydrates that provide energy to the body, particularly through glucose, a simple sugar that is a component of starch and an ingredient in many staple foods. The stoichiometric formula (CH2O)n, where n is the number of carbons in the molecule represents carbohydrates. In other words, the ratio of carbon to hydrogen to oxygen is 1:2:1 in carbohydrate molecules. This...
Chemistry of Carbohydrates03:25

Chemistry of Carbohydrates

Carbohydrates are an essential part of the diet in humans and animals. Grains, fruits, and vegetables are natural sources of carbohydrates that provide energy to the body, particularly through glucose, a simple sugar that is a component of starch and an ingredient in many staple foods. The stoichiometric formula (CH2O)n, where n is the number of carbons in the molecule represents carbohydrates. In other words, the ratio of carbon to hydrogen to oxygen is 1:2:1 in carbohydrate molecules. This...
Glycocalyx and its Functions01:14

Glycocalyx and its Functions

The glycocalyx is a carbohydrate-rich, fuzzy-appearing layer on the outer surface of the cell membrane. It is highly hydrophilic, because of this it attracts large amounts of water to the cell's surface. This aids the cell's interaction with the watery environment and also helps it to obtain substances dissolved in the water. It is also important for cell identification, self/non-self determination, and embryonic development and is used in cell-to-cell attachments to form tissues.
Components of...
Oligosaccharide Assembly01:24

Oligosaccharide Assembly

Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...

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Updated: May 29, 2026

Disentangling Glycan-Protein Interactions: Nuclear Magnetic Resonance (NMR) to the Rescue
07:40

Disentangling Glycan-Protein Interactions: Nuclear Magnetic Resonance (NMR) to the Rescue

Published on: May 17, 2024

Novel Click Coupling Chemistry to Explore Glycan Recognition.

Tianwei Jia1, Akul Y Mehta1, Catherine A Tilton1

  • 1Department of Surgery, Beth Israel Deaconess Medical Center, Harvard Medical School, National Center for Functional Glycomics, CLS 11087-3 Blackfan Circle, Boston, Massachusetts 02115, United States.

ACS Central Science
|June 2, 2025
PubMed
Summary

Researchers developed a new method to attach glycans to surfaces using click chemistry. This technique enables high-throughput analysis of glycan-protein interactions and antibody responses in human serum.

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Last Updated: May 29, 2026

Disentangling Glycan-Protein Interactions: Nuclear Magnetic Resonance (NMR) to the Rescue
07:40

Disentangling Glycan-Protein Interactions: Nuclear Magnetic Resonance (NMR) to the Rescue

Published on: May 17, 2024

Visualizing Intracellular Sialylation with Click Chemistry and Expansion Microscopy
08:16

Visualizing Intracellular Sialylation with Click Chemistry and Expansion Microscopy

Published on: February 7, 2025

Chemoselective Modification of Viral Surfaces via Bioorthogonal Click Chemistry
12:31

Chemoselective Modification of Viral Surfaces via Bioorthogonal Click Chemistry

Published on: August 19, 2012

Area of Science:

  • Carbohydrate Chemistry
  • Bioconjugation
  • Immunology

Background:

  • Specific recognition of glycans by proteins is crucial for biological processes and immune responses.
  • Existing methods for studying glycan-protein interactions can be limited in scope and throughput.

Purpose of the Study:

  • To develop a versatile and efficient method for derivatizing glycans for broad applications in biological research.
  • To create platforms for high-throughput screening of glycan-binding proteins and antibody responses.

Main Methods:

  • Developed a novel linker (MTZ) for bioorthogonal click chemistry-based glycan derivatization.
  • Created multiplex arrays using MTZ-glycans conjugated to Luminex beads.
  • Generated neoglycoproteins by coupling glycans to bovine serum albumin (BSA).

Main Results:

  • Efficiently generated libraries of ABO-(H) blood group MTZ-glycans and neoglycoproteins.
  • Successfully profiled antiglycan IgG, IgM, and IgA antibodies in human serum samples.
  • Demonstrated the utility of neoglycoproteins in glycosyltransferase assays.

Conclusions:

  • The MTZ linker and click chemistry approach provide a facile and efficient platform for exploring glycan-protein interactions.
  • This technology expands the available tools for studying glycan recognition in biological and immunological contexts.
  • The developed methods enable high-throughput analysis of glycan-specific antibody repertoires.