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dc.contributor.authorSheng, Anran
dc.contributor.authorChen, Qingqing
dc.contributor.authorYu, Mengqi
dc.contributor.authorXiao, Ruiqi
dc.contributor.authorZhang, Tianji
dc.contributor.authorWang, Zhiyu
dc.contributor.authorLinhardt, Robert J.
dc.contributor.authorSun, Xiaojun
dc.contributor.authorJin, Lan
dc.contributor.authorChi, Lianli
dc.date2021
dc.date.accessioned2022-06-27T15:38:39Z
dc.date.available2022-06-27T15:38:39Z
dc.date.issued2021-01-26
dc.identifier.citationCoupling liquid chromatography and tandem mass spectrometry to electrophoresis for in-depth analysis of glycosaminoglycan drugs: heparin and the multicomponent sulodexide, A. Sheng, Q. Chen, M. Yu, R. Xiao, T. Zhang, Z. Wang, R. J. Linhardt, X. Sun, L. Jin, L. Chi, Analytical Chemistry, 93, 1433−1442, 2021.
dc.identifier.issn15206882
dc.identifier.issn32700
dc.identifier.urihttps://doi.org/10.1021/acs.analchem.0c03330
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5465
dc.descriptionAnalytical Chemistry, 93, 1433−1442
dc.descriptionNote : 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.
dc.description.abstractGlycosaminoglycans (GAGs) contribute to the treatment of many human diseases, especially in the field of thrombosis, because of their anticoagulant activity. GAGs interrupt the coagulation process by interacting with multiple coagulation factors through defined sequences within their linear and negatively charged chains, which are not fully elucidated. Numerous methods have been developed to characterize the structure of pharmaceutical GAGs, including intravenously or subcutaneously administered heparin and orally administered sulodexide. However, most currently available methods only focus on the oligosaccharide portion or analyze the whole mixture because longer-chain polysaccharides are extremely difficult to resolve by chromatographic separation. We have established two novel electrophoresis–mass spectrometry methods to provide a panoramic view of the structures of pharmaceutical GAGs. In the first method, an in-gel digestion procedure was developed to recover GAGs from the polyacrylamide gels, while in the second method, a strong anion exchange ultrafiltration procedure was developed to extract multiple GAG species from the agarose gels. Both procedures are compatible with liquid chromatography–tandem mass spectrometry, and structural information, such as disaccharide composition and chain length, can be revealed for each GAG fraction. The applications of these two methods on analysis of two different GAG drugs, heparin and sulodexide, were demonstrated. The current study offers the first robust tool to directly elucidate the structure of larger GAG chains with more biological importance rather than obtaining a vague picture of all chains as a mixture, which is fundamental for better understanding the structure–activity relationship and quality control of the GAG drugs.
dc.description.sponsorshipFundamental Research Fund of Shandong University
dc.description.urihttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1021/acs.analchem.0c03330
dc.languageen_US
dc.language.isoENG
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofAnalytical Chemistry
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleCoupling liquid chromatography and tandem mass spectrometry to electrophoresis for in-depth analysis of glycosaminoglycan drugs: heparin and the multicomponent sulodexide
dc.typeArticle
dcterms.accessRightshttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1021/acs.analchem.0c03330
dcterms.isPartOfJournal
dcterms.isVersionOfhttps://doi.org/10.1021/acs.analchem.0c03330
dc.rights.holderIn Copyright : this Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s). https://rightsstatements.org/page/InC/1.0/
dc.creator.identifierhttps://orcid.org/0000-0003-2219-5833
dc.relation.departmentThe Linhardt Research Labs.
dc.relation.departmentThe Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
rpi.description.pages1433-1442
rpi.description.volume93


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