Electron Detachment Dissociation of Dermatan Sulfate Oligosaccharides
Authors
Wolff, Jeremy J.
Laremore, Tatiana N.
Busch, Alexander M.
Linhardt, Robert J.
Amster, I. Jonathan
ORCID
https://orcid.org/0000-0003-2219-5833
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Other Contributors
Issue Date
2008-02-01
Keywords
Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
Degree
Terms of Use
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Full Citation
Electron Detachment Dissociation of Dermatan Sulfate Oligosaccharides, J. J. Wolff, T. N. Laremore, A. M. Busch, R. J. Linhardt, I. Jonathan Amster, Journal of American Society of Mass Spectrometry, 19, 294-304, 2008.
Abstract
The structural characterization of glycosaminoglycans (GAG) oligosaccharides has been a long-standing challenge in the field of mass spectrometry. In this work, we present the application of electron detachment dissociation (EDD) Fourier transform mass spectrometry to the analysis of dermatan sulfate (DS) oligosaccharides up to 10 residues long. The EDD mass spectra of DS oligosaccharides were compared with their infrared multiphoton dissociation (IRMPD) mass spectra. EDD produces more abundant fragmentation than IRMPD with far less loss of SO3 from labile sulfate modifications. EDD cleaves all glycosidic bonds, yielding both conventional glycosidic bond fragmentation as well as satellite peaks resulting from the additional loss of 1 or 2 hydrogen atoms. EDD also yields more cross-ring fragmentation than IRMPD. For EDD, abundant cross-ring fragmentation in the form of A- and X-ions is observed, with 1,5Xn cleavages occurring for all IdoA residues and many of the GalNAc4S residues, except at the reducing and nonreducing ends. In contrast, IRMPD produces only A-type cross-ring fragmentation for long oligosaccharides (dp6-dp10). As all the structurally informative fragment ions observed by IRMPD appear as a subset of the peaks found in the EDD mass spectrum, EDD shows great potential for the characterization of GAG oligosaccharides using a single tandem mass spectrometry experiment.
Description
Journal of American Society of Mass Spectrometry, 19, 294-304
Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
Department
The Linhardt Research Labs.
The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
Publisher
American Chemical Society (ACS)
Relationships
The Linhardt Research Labs Online Collection
Rensselaer Polytechnic Institute, Troy, NY
Journal of the American Society for Mass Spectrometry
https://harc.rpi.edu/
Rensselaer Polytechnic Institute, Troy, NY
Journal of the American Society for Mass Spectrometry
https://harc.rpi.edu/
Access
A full text version is available in DSpace@RPI