Please use this identifier to cite or link to this item: http://hdl.handle.net/123456789/1201
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dc.contributor.authorSampathkumar, Srinivasa-Gopalan-
dc.contributor.authorRoy, Rajendra P-
dc.contributor.authorSingh, Shikha-
dc.contributor.authorGupta, Kanchan-
dc.contributor.authorShukla, Shagun-
dc.date.accessioned2021-03-23T09:52:10Z-
dc.date.available2021-03-23T09:52:10Z-
dc.date.issued2019-05-
dc.identifier.urihttp://hdl.handle.net/123456789/1201-
dc.description.abstractMultivalent proteins or protein dendrimers are useful for clinical and biotechnological applications. However, assembly of chemically defined protein dendrimers is a challenging endeavor. In the past, majority of protein dendrimers have been developed on branched lysine scaffolds and are usually limited to a valency of two to four. The naturally occurring cyclodextrin (CD) scaffold composed of 6-8 glucose units offers the possibility of expanding the valency. Here we have adapted a chemoenzymatic-click strategy for displaying heptavalent peptides and large proteins on the β-cyclodextrin (β-CD) scaffold. We demonstrate that recombinant proteins (engineered with a LPXTG pentapeptide motif at the carboxy terminus), labeled with an alkyne moiety by sortase-mediated ligation, can be easily clicked on to the azide-derivatized β-cyclodextrin through the Huisgen cycloaddition reaction yielding a well-defined heptavalent display of proteins.en_US
dc.language.isoenen_US
dc.publisherPLOSen_US
dc.titleSortase-click strategy for defined protein conjugation on a heptavalent cyclodextrin scaffolden_US
dc.typeArticleen_US
dc.journalPLoS Oneen_US
dc.volumeno14en_US
dc.issueno5en_US
dc.pagese0217369en_US
Appears in Collections:Chemical Glycobiology, Publications

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