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dc.contributor.authorMarks, R.M.
dc.contributor.authorLu, H.
dc.contributor.authorSundaresan, R.
dc.contributor.authorToida, T.
dc.contributor.authorSuzuki, A.
dc.contributor.authorImanari, T.
dc.contributor.authorHernaiz, M.J.
dc.contributor.authorLinhardt, Robert J.
dc.date2001
dc.date.accessioned2022-06-27T16:20:27Z
dc.date.available2022-06-27T16:20:27Z
dc.date.issued2001-06-21
dc.identifier.citationProbing the Interaction of Dengue Virus Envelope Protein with Heparin: Assessment of Glycosaminoglycan-Derived Inhibitors, R.M. Marks, H. Lu, R. Sundaresan, T. Toida, A. Suzuki, T. Imanari, M.J. Hernaiz, R. J. Linhardt, Journal of Medicinal Chemistry, 44, 2178-2187, 2001.
dc.identifier.issn222623
dc.identifier.urihttps://doi.org/10.1021/jm000412i
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5862
dc.descriptionJournal of Medicinal Chemistry, 44, 2178-2187
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.abstractA structure-activity relationship study was carried out to facilitate development of inhibitors of dengue virus infectivity. Previous studies demonstrated that a highly charged heparan sulfate, a heparin-like glycosaminoglycan found on the cell surface, serves as a receptor for dengue virus by binding to its envelope protein. Interventions that disrupt this binding effectively inhibit infectivity. A competitive binding assay was developed to screen polyanionic compounds for activity in preventing binding of dengue virus envelope protein to immobilized heparin; compounds tested included drugs, excipients, and larger glycosaminoglycans and their semisynthetic derivatives. Results of this competitive binding assay were used to select agents for detailed evaluation of interactions by surface plasmon resonance spectroscopy, which afforded binding on-rates, off-rates, and dissociation constants. From these data, an understanding of the structural requirements for polyanion binding to dengue virus envelope protein has been established.
dc.description.sponsorshipNational Heart, Lung, and Blood Institute
dc.description.urihttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1021/jm000412i
dc.languageen_US
dc.language.isoENG
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofJournal of Medicinal Chemistry
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleProbing the Interaction of Dengue Virus Envelope Protein with Heparin: Assessment of Glycosaminoglycan-Derived Inhibitors
dc.typeArticle
dcterms.accessRightshttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1021/jm000412i
dcterms.isPartOfJournal
dcterms.isVersionOfhttps://doi.org/10.1021/jm000412i
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.pages2178-2187
rpi.description.volume44


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