AuthorWolff, Jeremy J.; Laremore, Tatiana N.; Leach, Franklin E.; Linhardt, Robert J.; Amster, I. Jonathan
SubjectBiology; Chemistry and chemical biology; Chemical and biological engineering; Biomedical engineering
Full CitationElectron Capture Dissociation, Electron Detachment Dissociation, and Infrared Multiphoton Dissociation of Sucrose Octasulfate, J. J.Wolff, T. N.Laremore, F. E.Leach, R. J. Linhardt, I. Amster, European Journal of Mass Spectrometry, 15, 275–281, 2009.
AbstractThe structural analysis of sulfated carbohydrates such as glycosaminoglycans (GAGs) has been a long- standing challenge for the field of mass spectrometry. The dissociation of sulfated carbohydrates by collisionally- activated dissociation (CAD) or infrared multiphoton dissociation (IRMPD), which activate ions via vibrational excitation, typically result in few cleavages and abundant SO(3) loss for highly sulfated GAGs such as heparin and heparan sulfate, hampering efforts to determine sites of modification. The recent application of electron activation techniques, specifically electron capture dissociation (ECD) and electron detachment dissociation (EDD), provides a marked improvement for the mass spectrometry characterization of GAGs. In this work, we compare ECD, EDD and IRMPD for the dissociation of the highly sulfated carbohydrate sucrose octasulfate (SOS). Both positive and negative multiply-charged ions are investigated. ECD, EDD and IRMPD of SOS produce abundant and reproducible fragmentation. The product ions produced by ECD are quite different than those produced by IRMPD of SOS positive ions, suggesting different dissociation mechanisms as a result of electronic versus vibrational excitation. The product ions produced by EDD and IRMPD of SOS negative ions also differ from each other. Evidence for SO(3) rearrangement exists in the negative ion IRMPD data, complicating the assignment of product ions.;
DescriptionEuropean Journal of Mass Spectrometry, 15, 275–281; 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.
DepartmentThe Linhardt Research Labs.; The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS);
RelationshipsThe Linhardt Research Labs Online Collection; Rensselaer Polytechnic Institute, Troy, NY; European Journal of Mass Spectrometry; https://harc.rpi.edu/;
AccessA full text version is available in DSpace@RPI;