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

Research output: Contribution to journal › Journal article › Research › peer-review

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Direct observation of glycans bonded to proteins and lipids at the single-molecule level. / Anggara, Kelvin; Sršan, Laura; Jaroentomeechai, Thapakorn; Wu, Xu; Rauschenbach, Stephan; Narimatsu, Yoshiki; Clausen, Henrik; Ziegler, Thomas; Miller, Rebecca L; Kern, Klaus.

In: Science (New York, N.Y.), Vol. 382, No. 6667, 2023, p. 219-223.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Anggara, K, Sršan, L, Jaroentomeechai, T, Wu, X, Rauschenbach, S, Narimatsu, Y, Clausen, H, Ziegler, T, Miller, RL & Kern, K 2023, 'Direct observation of glycans bonded to proteins and lipids at the single-molecule level', Science (New York, N.Y.), vol. 382, no. 6667, pp. 219-223. https://doi.org/10.1126/science.adh3856

APA

Anggara, K., Sršan, L., Jaroentomeechai, T., Wu, X., Rauschenbach, S., Narimatsu, Y., Clausen, H., Ziegler, T., Miller, R. L., & Kern, K. (2023). Direct observation of glycans bonded to proteins and lipids at the single-molecule level. Science (New York, N.Y.), 382(6667), 219-223. https://doi.org/10.1126/science.adh3856

Vancouver

Anggara K, Sršan L, Jaroentomeechai T, Wu X, Rauschenbach S, Narimatsu Y et al. Direct observation of glycans bonded to proteins and lipids at the single-molecule level. Science (New York, N.Y.). 2023;382(6667):219-223. https://doi.org/10.1126/science.adh3856

Author

Anggara, Kelvin ; Sršan, Laura ; Jaroentomeechai, Thapakorn ; Wu, Xu ; Rauschenbach, Stephan ; Narimatsu, Yoshiki ; Clausen, Henrik ; Ziegler, Thomas ; Miller, Rebecca L ; Kern, Klaus. / Direct observation of glycans bonded to proteins and lipids at the single-molecule level. In: Science (New York, N.Y.). 2023 ; Vol. 382, No. 6667. pp. 219-223.

Bibtex

@article{e8da75bdea8a48399cc5185577dbb1c4,

title = "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.",

keywords = "Glycoconjugates/chemistry, Glycolipids/chemistry, Glycoproteins/chemistry, Polysaccharides/chemistry, Single Molecule Imaging, Mucin-1/chemistry",

author = "Kelvin Anggara and Laura Sr{\v s}an and Thapakorn Jaroentomeechai and Xu Wu and Stephan Rauschenbach and Yoshiki Narimatsu and Henrik Clausen and Thomas Ziegler and Miller, {Rebecca L} and Klaus Kern",

year = "2023",

doi = "10.1126/science.adh3856",

language = "English",

volume = "382",

pages = "219--223",

journal = "Science",

issn = "0036-8075",

publisher = "American Association for the Advancement of Science",

number = "6667",

}

RIS

TY - JOUR

T1 - Direct observation of glycans bonded to proteins and lipids at the single-molecule level

AU - Anggara, Kelvin

AU - Sršan, Laura

AU - Jaroentomeechai, Thapakorn

AU - Wu, Xu

AU - Rauschenbach, Stephan

AU - Narimatsu, Yoshiki

AU - Clausen, Henrik

AU - Ziegler, Thomas

AU - Miller, Rebecca L

AU - Kern, Klaus

PY - 2023

Y1 - 2023

N2 - 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.

AB - 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.

KW - Glycoconjugates/chemistry

KW - Glycolipids/chemistry

KW - Glycoproteins/chemistry

KW - Polysaccharides/chemistry

KW - Single Molecule Imaging

KW - Mucin-1/chemistry

U2 - 10.1126/science.adh3856

DO - 10.1126/science.adh3856

M3 - Journal article

C2 - 37824645

VL - 382

SP - 219

EP - 223

JO - Science

JF - Science

SN - 0036-8075

IS - 6667

ER -

ID: 381147304