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From the same journal

A protein-based pentavalent inhibitor of the Cholera toxin B-subunit

Research output: Contribution to journalArticlepeer-review


  • Thomas R. Branson
  • Tom E. McAllister
  • Jaime Garcia-Hartjes
  • Martin Anthony Fascione
  • James F. Ross
  • Stuart L. Warriner
  • Tom Wennekes
  • Hans Zuilhof
  • Bruce Turnbull


Publication details

JournalAngewandte Chemie International Edition
DateE-pub ahead of print - 2 Jul 2014
DatePublished (current) - 4 Aug 2014
Issue number32
Number of pages5
Pages (from-to)8323-8327
Early online date2/07/14
Original languageEnglish


Protein toxins produced by bacteria are the cause of many life-threatening diarrheal diseases. Many of these toxins, including cholera toxin (CT), enter the cell by first binding to glycolipids in the cell membrane. Inhibiting these multivalent protein/carbohydrate interactions would prevent the toxin from entering cells and causing diarrhea. Here we demonstrate that the site-specific modification of a protein scaffold, which is perfectly matched in both size and valency to the target toxin, provides a convenient route to an effective multivalent inhibitor. The resulting pentavalent neoglycoprotein displays an inhibition potency (IC50) of 104 pm for the CT B-subunit (CTB), which is the most potent pentavalent inhibitor for this target reported thus far. Complexation of the inhibitor and CTB resulted in a protein heterodimer. This inhibition strategy can potentially be applied to many multivalent receptors and also opens up new possibilities for protein assembly strategies.

    Research areas

  • carbohydrates;glycoproteins;multivalency;protein modifications;protein structures

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