ArticlePloS one2019
Sortase-click strategy for defined protein conjugation on a heptavalent cyclodextrin scaffold.
Article in PloS one, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed.
- Advances in polyethylene biodegradation and bioconversion: Microbial, enzymatic, and biotechnological insights.Engineering microbiology · 2026Review
- Click Chemistry as an Efficient Toolbox for Coupling Sterically Hindered Molecular Systems to Obtain Advanced Materials for Nanomedicine.International journal of molecular sciences · 2024Review
- Leveraging immunoliposomes as nanocarriers against SARS-CoV-2 and its emerging variants.Asian journal of pharmaceutical sciences · 2023Review
- Review
- Protein engineering strategies for rational immunogen design.NPJ vaccines · 2021Review
- Review
- Picomolar SARS-CoV-2 Neutralization Using Multi-Arm PEG Nanobody Constructs.Biomolecules · 2020Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Multivalent 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.
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Registered trials
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