dc.contributor.author
Kirschbaum, Carla
dc.contributor.author
Greis, Kim
dc.contributor.author
Mucha, Eike
dc.contributor.author
Kain, Lisa
dc.contributor.author
Deng, Shenglou
dc.contributor.author
Zappe, Andreas
dc.contributor.author
Gewinner, Sandy
dc.contributor.author
Schöllkopf, Wieland
dc.contributor.author
Helden, Gert von
dc.contributor.author
Pagel, Kevin
dc.date.accessioned
2021-03-22T08:22:02Z
dc.date.available
2021-03-22T08:22:02Z
dc.identifier.uri
https://refubium.fu-berlin.de/handle/fub188/30113
dc.identifier.uri
http://dx.doi.org/10.17169/refubium-29855
dc.description.abstract
Glycolipids are complex glycoconjugates composed of a glycan headgroup and a lipid moiety. Their modular biosynthesis creates a vast amount of diverse and often isomeric structures, which fulfill highly specific biological functions. To date, no gold-standard analytical technique can provide a comprehensive structural elucidation of complex glycolipids, and insufficient tools for isomer distinction can lead to wrong assignments. Herein we use cryogenic gas-phase infrared spectroscopy to systematically investigate different kinds of isomerism in immunologically relevant glycolipids. We show that all structural features, including isomeric glycan headgroups, anomeric configurations and different lipid moieties, can be unambiguously resolved by diagnostic spectroscopic fingerprints in a narrow spectral range. The results allow for the characterization of isomeric glycolipid mixtures and biological applications.
en
dc.format.extent
7 Seiten
dc.rights.uri
https://creativecommons.org/licenses/by/4.0/
dc.subject
Glycobiology
en
dc.subject
Infrared spectroscopy
en
dc.subject.ddc
500 Naturwissenschaften und Mathematik::570 Biowissenschaften; Biologie::570 Biowissenschaften; Biologie
dc.title
Unravelling the structural complexity of glycolipids with cryogenic infrared spectroscopy
dc.type
Wissenschaftlicher Artikel
dcterms.bibliographicCitation.articlenumber
1201
dcterms.bibliographicCitation.doi
10.1038/s41467-021-21480-1
dcterms.bibliographicCitation.journaltitle
Nature Communications
dcterms.bibliographicCitation.volume
12
dcterms.bibliographicCitation.url
https://doi.org/10.1038/s41467-021-21480-1
refubium.affiliation
Biologie, Chemie, Pharmazie
refubium.affiliation.other
Institut für Chemie und Biochemie
refubium.funding
Springer Nature DEAL
refubium.note.author
Die Publikation wurde aus Open Access Publikationsgeldern der Freien Universität Berlin gefördert.
refubium.resourceType.isindependentpub
no
dcterms.accessRights.openaire
open access
dcterms.isPartOf.eissn
2041-1723