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dc.contributor.authorA. Chokhawala, Harshalen_US
dc.contributor.authorHuang, Shengshuen_US
dc.contributor.authorLau, Kamen_US
dc.contributor.authorYu, Haien_US
dc.contributor.authorCheng, Jiansongen_US
dc.contributor.authorThon, Vireaken_US
dc.contributor.authorHurtado-Ziola, Nancyen_US
dc.contributor.authorA. Guerrero, Juanen_US
dc.contributor.authorVarki, Ajiten_US
dc.contributor.authorChen, Xien_US
dc.date.accessioned2017-04-24T13:30:58Z
dc.date.available2017-04-24T13:30:58Z
dc.date.issued2008en_US
dc.date.modified2011-05-03T04:47:23Z
dc.identifier.issn15548937en_US
dc.identifier.doi10.1021/cb800127nen_AU
dc.identifier.urihttp://hdl.handle.net/10072/38543
dc.description.abstractAlthough the vital roles of structures containing sialic acid in biomolecular recognition are well documented, limited information is available on how sialic acid structural modifications, sialyl linkages, and the underlying glycan structures affect the binding or the activity of sialic acid-recognizing proteins and related downstream biological processes. A novel combinatorial chemoenzymatic method has been developed for the highly efficient synthesis of biotinylated sialosides containing different sialic acid structures and different underlying glycans in 96-well plates from biotinylated sialyltransferase acceptors and sialic acid precursors. By transferring the reaction mixtures to NeutrAvidin-coated plates and assaying for the yields of enzymatic reactions using lectins recognizing sialyltransferase acceptors but not the sialylated products, the biotinylated sialoside products can be directly used, without purification, for high-throughput screening to quickly identify the ligand specificity of sialic acid-binding proteins. For a proof-of-principle experiment, 72 biotinylated a2,6-linked sialosides were synthesized in 96-well plates from 4 biotinylated sialyltransferase acceptors and 18 sialic acid precursors using a one-pot three-enzyme system. High-throughput screening assays performed in NeutrAvidin-coated microtiter plates show that whereas Sambucus nigra Lectin binds to a2,6-linked sialosides with high promiscuity, human Siglec-2 (CD22) is highly selective for a number of sialic acid structures and the underlying glycans in its sialoside ligands.en_US
dc.description.peerreviewedYesen_US
dc.description.publicationstatusYesen_AU
dc.languageEnglishen_US
dc.language.isoen_AU
dc.publisherAmerican Chemical Societyen_US
dc.publisher.placeUnited Statesen_US
dc.relation.ispartofstudentpublicationNen_AU
dc.relation.ispartofpagefrom567en_US
dc.relation.ispartofpageto576en_US
dc.relation.ispartofissue9en_US
dc.relation.ispartofjournalACS Chemical Biologyen_US
dc.relation.ispartofvolume3en_US
dc.rights.retentionYen_AU
dc.subject.fieldofresearchOrganic Chemical Synthesisen_US
dc.subject.fieldofresearchcode030503en_US
dc.titleCombinatorial Chemoenzymatic Synthesis and High-throughput Screening of Sialosidesen_US
dc.typeJournal articleen_US
dc.type.descriptionC1 - Peer Reviewed (HERDC)en_US
dc.type.codeC - Journal Articlesen_US
gro.rights.copyrightSelf-archiving of the author-manuscript version is not yet supported by this journal. Please refer to the journal link for access to the definitive, published version or contact the authors for more information.en_AU
gro.date.issued2008
gro.hasfulltextNo Full Text


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