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

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 vie...

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Main Authors: Anggara, K, Sršan, L, Jaroentomeechai, T, Wu, X, Rauschenbach, S, Narimatsu, Y, Clausen, H, Ziegler, T, Miller, RL, Kern, K
Format: Journal article
Language:English
Published: American Association for the Advancement of Science 2023
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author Anggara, K
Sršan, L
Jaroentomeechai, T
Wu, X
Rauschenbach, S
Narimatsu, Y
Clausen, H
Ziegler, T
Miller, RL
Kern, K
author_facet Anggara, K
Sršan, L
Jaroentomeechai, T
Wu, X
Rauschenbach, S
Narimatsu, Y
Clausen, H
Ziegler, T
Miller, RL
Kern, K
author_sort Anggara, K
collection OXFORD
description 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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spelling oxford-uuid:eb730070-a5be-494d-9927-27957490122b2023-10-23T10:58:48ZDirect observation of glycans bonded to proteins and lipids at the single-molecule levelJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:eb730070-a5be-494d-9927-27957490122bEnglishSymplectic ElementsAmerican Association for the Advancement of Science2023Anggara, KSršan, LJaroentomeechai, TWu, XRauschenbach, SNarimatsu, YClausen, HZiegler, TMiller, RLKern, KProteins 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.
spellingShingle Anggara, K
Sršan, L
Jaroentomeechai, T
Wu, X
Rauschenbach, S
Narimatsu, Y
Clausen, H
Ziegler, T
Miller, RL
Kern, K
Direct observation of glycans bonded to proteins and lipids at the single-molecule level
title Direct observation of glycans bonded to proteins and lipids at the single-molecule level
title_full Direct observation of glycans bonded to proteins and lipids at the single-molecule level
title_fullStr Direct observation of glycans bonded to proteins and lipids at the single-molecule level
title_full_unstemmed Direct observation of glycans bonded to proteins and lipids at the single-molecule level
title_short Direct observation of glycans bonded to proteins and lipids at the single-molecule level
title_sort direct observation of glycans bonded to proteins and lipids at the single molecule level
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