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dc.contributor.authorHorton, Maurice
dc.contributor.authorSu, Guowei
dc.contributor.authorYi, Lin
dc.contributor.authorWang, Zhangjie
dc.contributor.authorXu, Yongmei
dc.contributor.authorPagadala, Vijayakanth
dc.contributor.authorZhang, Fuming
dc.contributor.authorZaharoff, David A.
dc.contributor.authorPearce, Ken
dc.contributor.authorLinhardt, Robert J.
dc.contributor.authorLiu, Jian
dc.date2021
dc.date.accessioned2022-06-27T15:36:57Z
dc.date.available2022-06-27T15:36:57Z
dc.date.issued2021-03-01
dc.identifier.citationConstruction of heparan sulfate microarray for investigating the binding of specific saccharide sequences to proteins, M. Horton, G. Su, L. Yi, Y. Xu, V. Pagadala, F. Zhang, K. Pierce, R. J Linhardt, J. Liu, Glycobiology, 31, 188–199, 2021.
dc.identifier.issn14602423
dc.identifier.issn9596658
dc.identifier.urihttps://doi.org/10.1093/glycob/cwaa068
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5450
dc.descriptionGlycobiology, 31, 188–199
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.abstractHeparan sulfate (HS) is a heterogeneous, extracellular glycan that interacts with proteins and other molecules affecting many biological processes. The specific binding motifs of HS interactions are of interest, but have not been extensively characterized. Glycan microarrays are valuable tools that can be used to probe the interactions between glycans and their ligands while relying on relatively small amounts of samples. Recently, chemoenzymatic synthesis of HS has been employed to produce specific HS structures that can otherwise be difficult to produce. In this study, a microarray of diverse chemoenzymatically synthesized HS structures was developed and HS interactions were characterized. Fluorescently labeled antithrombin III (AT) and fibroblast growth factor-2 (FGF2) were screened against 95 different HS structures under three different printing concentrations to confirm the utility of this microarray. Specific sulfation patterns were found to be important for binding to these proteins and results are consistent with previous specificity studies. Furthermore, the binding affinities (KD,surf) of AT and FGF2 to multiple HS structures were determined using a microarray technique and is consistent with previous reports. Lastly, the 95-compound HS microarray was used to determine the distinct binding profiles for interleukin 12 and platelet factor 4. This technique is ideal for rapid expansion and will be pivotal to the high-throughput characterization of biologically important structure/function relationships.
dc.languageen_US
dc.language.isoENG
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofGlycobiology
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleConstruction of heparan sulfate microarray for investigating the binding of specific saccharide sequences to proteins
dc.typeArticle
dcterms.isPartOfJournal
dcterms.isVersionOfhttps://doi.org/10.1093/glycob/cwaa068
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.pages188-199
rpi.description.volume31


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