Show simple item record

dc.contributor.authorYan, Lufeng
dc.contributor.authorLi, Junhui
dc.contributor.authorWang, Danli
dc.contributor.authorDing, Tian
dc.contributor.authorHu, Yaqin
dc.contributor.authorYe, Xingqian
dc.contributor.authorLinhardt, Robert J.
dc.contributor.authorChen, Shiguo
dc.date2017
dc.date.accessioned2022-06-27T15:52:27Z
dc.date.available2022-06-27T15:52:27Z
dc.date.issued2017-12-15
dc.identifier.citationMolecular size is important for the safety and selective inhibition of intrinsic factor Xase for fucosylated chondroitin sulfate, L. Yan, J. Li, D. Wang, D. Tian, Y. Hu, X. Ye, R. J. Linhardt, S. Chen, Carbohydrate Polymers, 178, 180-189, 2017.
dc.identifier.issn1448617
dc.identifier.urihttps://doi.org/10.1016/j.carbpol.2017.09.034
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5611
dc.descriptionCarbohydrate Polymers, 178, 180-189
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.abstractFucosylated chondroitin sulfate from sea cucumber Isostichopus badionotus (FCS-Ib) showed potent anticoagulant activities without selectivity. The present study focused on developing safe FCS-Ib oligomers showing selective inhibition of intrinsic factor Xase (anti-FXase) prepared through partial N-deacetylation-deaminative cleavage. The N-deacetylation degree was regulated by reaction time, controlling the resulting oligomer distribution. Structure analysis confirmed the selectivity of degradation, and 12 high purity fractions with trisaccharide-repeating units were separated. In vitro anticoagulant assays indicated a decrease in molecular weight (Mw) dramatically reduced activated partial thromboplastin time (APTT), thrombin time (TT), AT-dependent anti-FIIa and anti-FXa activities, while the oligomers retained potent anti-FXase activity until they fell below 3kDa. Meanwhile, human FXII activation and platelet aggregation were markedly reduced with decreasing Mw and were moderate when under 12.0kDa. Thus, fragments of 3-12.0kDa should be safe and effective as selective inhibitors of intrinsic tenase complex for application as clinical anticoagulants.
dc.description.sponsorshipNational Natural Science Foundation of China
dc.description.urihttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1016/j.carbpol.2017.09.034
dc.languageen_US
dc.language.isoENG
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofCarbohydrate Polymers
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleMolecular size is important for the safety and selective inhibition of intrinsic factor Xase for fucosylated chondroitin sulfate
dc.typeArticle
dcterms.accessRightshttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1016/j.carbpol.2017.09.034
dcterms.isPartOfJournal
dcterms.isVersionOfhttps://doi.org/10.1016/j.carbpol.2017.09.034
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.pages180-189
rpi.description.volume178


Files in this item

FilesSizeFormatView

There are no files associated with this item.

This item appears in the following Collection(s)

Show simple item record