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


ABSTRACT: 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.

SUBMITTER: Anggara K 

PROVIDER: S-EPMC7615228 | biostudies-literature | 2023 Oct

REPOSITORIES: biostudies-literature

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

Anggara Kelvin K   Sršan Laura L   Jaroentomeechai Thapakorn T   Wu Xu X   Rauschenbach Stephan S   Narimatsu Yoshiki Y   Clausen Henrik H   Ziegler Thomas T   Miller Rebecca L RL   Kern Klaus K  

Science (New York, N.Y.) 20231012 6667


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 indivi  ...[more]

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