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Related Experiment Video

Updated: Jul 5, 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

Exploration of mucin-protein interactions using liquid glycan array.

Shreyas Gupta¹, Guilherme Meira Lima¹, Chuanhao Peng¹

¹Department of Chemistry, University of Alberta, Edmonton, AB, Canada.

Methods in Enzymology

|July 3, 2026

Summary

DNA-barcoded M13 phages create a Liquid Glycan Array (LiGA) to profile mucin-binding proteins. Ultra-dense D-galactose displays mimic mucin, binding specifically to a mucinase mutant.

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Area of Science:

Biotechnology
Molecular Biology
Glycobiology

Background:

M13 phage can display molecules via DNA-barcoding, enabling a 1:1 link between displayed molecule and DNA sequence.
This DNA-encoded display allows for controlled multivalency, where DNA barcodes correlate with displayed density.

Purpose of the Study:

To develop a DNA-encoded multivalent system for glycan recognition profiling.
To investigate the binding properties of mucin-binding proteins using this novel system.

Main Methods:

Chemical conjugation of glycans to M13 virions with introduced DNA barcodes to create DNA-barcoded glycophages.
Utilizing a collection of these DNA-barcoded multivalent glycophages, termed Liquid Glycan Array (LiGA).
Testing the binding of mucinase StcE (StcE^E447D) to various ultra-dense displays of D-galactose and control sugars.

Keywords:

DNA-encoded multivalency Liquid glycan array M13 phage Phage-displayed glycans Protein-glycan interactions

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Last Updated: Jul 5, 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 Agarose Gel Electrophoresis: Western Blotting for High-molecular-weight Glycoproteins

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Published on: June 14, 2016

Microarray Polymer Profiling (MAPP) for High-Throughput Glycan Analysis

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Published on: September 29, 2023

Main Results:

LiGA successfully measured the glycan-recognition profile of mucin-binding proteins.
An ultra-dense display of D-galactose on M13 phages demonstrated binding to StcE^E447D, mimicking mucin.
Specificity was confirmed as StcE^E447D did not bind to L-galactose, D-glucose, or D-mannose displays.

Conclusions:

DNA-encoded multivalency using M13 phages (LiGA) is an effective tool for studying glycan-protein interactions.
Ultra-dense displays of specific glycans can present unique binding characteristics, as exemplified by D-galactose binding to StcE^E447D.
This approach offers a novel method for characterizing the specific recognition profiles of proteins like mucin-binding enzymes.