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research article

Direct observation of glycans bonded to proteins and lipids at the single-molecule level

Anggara, Kelvin
•
Srsan, Laura
•
Jaroentomeechai, Thapakorn
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October 13, 2023
Science

Proteins and lipids decorated with glycans are found throughout biological entities, playing roles in biological functions and dysfunctions. Current analytical strategies for these glycan-decorated biomolecules, termed glycoconjugates, rely on ensemble-averaged methods that do not provide a full view of positions and structures of glycans attached at individual sites in a given molecule, especially for glycoproteins. We show single-molecule analysis of glycoconjugates by direct imaging of individual glycoconjugate molecules using low-temperature scanning tunneling microscopy. Intact glycoconjugate ions from electrospray are soft-landed on a surface for their direct single-molecule imaging. The submolecular imaging resolution corroborated by quantum mechanical modeling unveils whole structures and attachment sites of glycans in glycopeptides, glycolipids, N-glycoproteins, and O-glycoproteins densely decorated with glycans.

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Type
research article
DOI
10.1126/science.adh3856
Web of Science ID

WOS:001112161200034

Author(s)
Anggara, Kelvin
•
Srsan, Laura
•
Jaroentomeechai, Thapakorn
•
Wu, Xu
•
Rauschenbach, Stephan
•
Narimatsu, Yoshiki
•
Clausen, Henrik
•
Ziegler, Thomas
•
Miller, Rebecca L.
•
Kern, Klaus  
Date Issued

2023-10-13

Publisher

American Association for the Advancement of Science

Published in
Science
Volume

382

Issue

6667

Start page

219

End page
Subjects

Mass-Spectrometry

•

Biological Roles

•

Glycosylation

•

Conformation

•

Surface

•

Oligosaccharides

•

Nanoelectrospray

•

Glycopeptides

•

Visualization

•

Specificity

Peer reviewed

REVIEWED

Written at

EPFL

EPFL units
LSEN  
FunderGrant Number

Alexander von Humboldt Foundation

Baden Wurttemberg Foundation Project GlycoPepSurf

European Research Council Project GlycoX grant

101075996

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Available on Infoscience
February 20, 2024
Use this identifier to reference this record
https://infoscience.epfl.ch/handle/20.500.14299/204487
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