Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Oligosaccharide Assembly

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...

Laminins are the Adhesive Proteins of Basal Lamina

Laminins are the Adhesive Proteins of Basal Lamina

Laminins are heterotrimeric proteins with high molecular mass found in the extracellular matrix. Each laminin molecule is composed of three chains, viz. alpha, beta, and gamma, coded by five, four, and three paralogous genes, respectively. Laminins are categories based on the compositions of the three chains.
In humans, the five forms of alpha chains are LAMA 1, LAMA 2, LAMA 3, LAMA 4, and LAMA 5. The four forms of beta chains are LAMB 1, LAMB 2, LAMB 3, and LAMB 4. The three forms of gamma...

Proteoglycans

Proteoglycans

Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...

Glycocalyx and its Functions

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...

Protein Glycosylation

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...

Tight Junctions

Tight Junctions

Tight junctions are molecular seals between cells that prevent the leaking of fluids, ions, and other small solutes across cavities and compartments in multicellular organisms. They are mainly composed of claudin and occludin transmembrane proteins, and other proteins such as tricellulin and JAM (junctional adhesion molecule). All these proteins are 4-pass transmembrane proteins, except JAM, which is a single-pass transmembrane protein belonging to the immunoglobulin superfamily. The...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Methods for studying mucin-microbe interactions.

Methods in enzymology·2026

Same author

Covalent crosslinking of mucins: From biomaterial design to tailored functions.

Methods in enzymology·2026

Same author

Mucin-induced metabolic reprogramming in <i>Pseudomonas aeruginosa</i> clinical isolates.

mSystems·2026

Same author

It's not just snot! : Mucus: Nature's Multifaceted Secretion.

EMBO reports·2026

Same author

Innovative microparticle strategies: harnessing essential oil-loaded lecithin/chitosan systems against <i>Burkholderia pseudomallei</i>.

Biofouling·2026

Same author

Correction to "Glyco-Modification of Mucin Hydrogels to Investigate Their Immune Activity".

ACS applied materials & interfaces·2026

Search research articles

Related Experiment Video

Updated: May 19, 2026

Profiling of Permethylated Mucin O-glycans Using Matrix-assisted Laser Desorption/Ionization Time-of-flight Mass Spectrometry

Profiling of Permethylated Mucin O-glycans Using Matrix-assisted Laser Desorption/Ionization Time-of-flight Mass Spectrometry

Published on: June 20, 2025

Mucin multilayers assembled through sugar-lectin interactions.

Thomas Crouzier¹, Colin H Beckwitt, Katharina Ribbeck

¹Department of Biological Engineering, Massachusetts Institute of Technology, Cambridge, MA, USA.

Biomacromolecules

|August 28, 2012

Summary

This summary is machine-generated.

Researchers developed stable mucin multilayer films using wheat germ agglutinin (WGA) cross-linking. These functional biomaterial coatings offer exceptional pH and salt resistance, with controlled cargo release capabilities.

More Related Videos

Using Unfixed, Frozen Tissues to Study Natural Mucin Distribution

Using Unfixed, Frozen Tissues to Study Natural Mucin Distribution

Published on: September 21, 2012

Mucin Agarose Gel Electrophoresis: Western Blotting for High-molecular-weight Glycoproteins

Mucin Agarose Gel Electrophoresis: Western Blotting for High-molecular-weight Glycoproteins

Published on: June 14, 2016

Related Experiment Videos

Last Updated: May 19, 2026

Profiling of Permethylated Mucin O-glycans Using Matrix-assisted Laser Desorption/Ionization Time-of-flight Mass Spectrometry

Profiling of Permethylated Mucin O-glycans Using Matrix-assisted Laser Desorption/Ionization Time-of-flight Mass Spectrometry

Published on: June 20, 2025

Using Unfixed, Frozen Tissues to Study Natural Mucin Distribution

Using Unfixed, Frozen Tissues to Study Natural Mucin Distribution

Published on: September 21, 2012

Mucin Agarose Gel Electrophoresis: Western Blotting for High-molecular-weight Glycoproteins

Mucin Agarose Gel Electrophoresis: Western Blotting for High-molecular-weight Glycoproteins

Published on: June 14, 2016

Area of Science:

Biomaterials Science
Surface Chemistry
Glycobiology

Background:

Multilayer films offer unique surface functionalities.
Mucins, versatile glycoproteins, are promising biomaterial building blocks.
Conventional polyelectrolyte films lack stability and payload binding sites.

Purpose of the Study:

To assemble stable mucin multilayer films distinct from conventional polyelectrolyte assemblies.
To achieve highly stable and functional surface modifications using mucins.
To explore the potential of mucin-based films for biomaterial applications.

Main Methods:

Assembly of mucin multilayer films using wheat germ agglutinin (WGA) as a cross-linker.
Utilizing lectin-carbohydrate interactions to cross-link mucin-bound sugar residues.
Investigating film stability under extreme pH and salt conditions.
Demonstrating controlled release of WGA and model cargo.

Main Results:

Successfully grew hydrated (Mucin/WGA) multilayer films.
Films exhibited exceptional resistance to extreme salt concentrations and a wide pH range.
Controlled release of WGA was induced by N-acetyl-d-glucosamine.
Films demonstrated repeated incorporation and release of a positively charged model cargo.

Conclusions:

Mucin/WGA films provide highly stable and functional surface modifications.
These films overcome limitations of conventional polyelectrolyte assemblies.
Mucin-based films offer diverse applicative perspectives due to their inherent properties.