Inside Cover: A Protein‐Based Pentavalent Inhibitor of the Cholera Toxin B‐Subunit (Angew. Chem. Int. Ed. 32/2014). Issue 32 (2nd July 2014)

• Record Type: Journal Article
• Authors: Branson, Thomas R.; McAllister, Tom E.; Garcia‐Hartjes, Jaime; Fascione, Martin A.; Ross, James F.; Warriner, Stuart L.; Wennekes, Tom; Zuilhof, Han; Turnbull, W. Bruce
• Is Part Of: Angewandte Chemie international edition. Volume 53:Issue 32(2014)
• Page Start: 8254
• Page End: 8254
• Publication Date: 2014-07-02
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201405672
• Languages: English
• ISSNs: 1433-7851

Abstract

<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>The cholera toxin B‐subunit has been re‐engineered to create a potent inhibitor of the parent toxin. Toxin adhesion can be blocked by a nonbinding mutant of the B subunit, which was modified with five copies of the carbohydrate ligand, as shown by W. B Turnbull and co‐workers in their Communication on <ext-link ext-link-type="doi" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink">page 8323 ff.</ext-link> Site‐specific modification of a protein scaffold that is matched in both size and valency to the target toxin may become a general strategy for inhibitor design.<boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pghwkxmz4j" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>