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dc.contributor.authorZhao, J.
dc.contributor.authorLiu, X.
dc.contributor.authorKao, C.
dc.contributor.authorZhang, E.
dc.contributor.authorLi, Q.
dc.contributor.authorZhang, F.
dc.contributor.authorLinhardt, Robert J.
dc.date2016
dc.date.accessioned2022-06-27T16:02:11Z
dc.date.available2022-06-27T16:02:11Z
dc.date.issued2016
dc.identifier.citationKinetic and Structural Studies on Interactions between Heparin/GAGs and Langerin, J. Zhao, X. Liu, C. Kao, E. Zhang, Q. Li, F. Zhang, R. J. Linhardt, Biochemistry, 55, 4552−4559, 2016.
dc.identifier.urihttps://doi.org/10.1021/acs.biochem.6b00555
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5653
dc.descriptionBiochemistry, 55, 4552−4559
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.abstractLangerin, a C-type lectin, is expressed in Langerhans cells. It was reported that langerin binds sulfated glycans, which is an important initial step for its role in blocking human immunodeficiency virus (HIV) transmission by capturing HIV pathogens and mediating their internalization into Birbeck granules for their elimination. It is fundamentally important to understand these interactions at the molecular level for the design of new highly specific therapeutic agents for HIV. Surface plasmon resonance (SPR), which allows for the real-time, direct, quantitative analysis of the label-free molecular interactions, has been used successfully for biophysical characterization of glycosaminoglycan (GAG)-protein interactions. In this study, we report kinetics, structural analysis, and the effects of physiological conditions (e.g., pH, salt concentration, and Ca(2+) and Zn(2+)concentrations) on the interactions between GAGs and langerin using SPR. SPR results revealed that langerin binds to heparin with high affinity (KD ∼ 2.4 nM) and the oligosaccharide length required for the interactions is larger than a tetrasaccharide. This heparin/heparan sulfate-binding protein also interacts with other GAGs, including dermatan sulfate, chondroitin sulfates C-E and KS. In addition, liquid chromatography-mass spectrometry analysis was used to characterize the structure of sulfated glycans that bound to langerin.
dc.description.urihttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1021/acs.biochem.6b00555
dc.languageen_US
dc.language.isoENG
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleKinetic and Structural Studies on Interactions between Heparin/GAGs and Langerin
dc.typeArticle
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dcterms.isVersionOfhttps://doi.org/10.1021/acs.biochem.6b00555
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)


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