Cover Feature: Photoswitching Affinity and Mechanism of Multivalent Lectin Ligands (Chem. Eur. J. 27/2022). Issue 27 (12th April 2022)

• Record Type: Journal Article
• Authors: Osswald, Uwe; Boneberg, Johannes; Wittmann, Valentin
• Is Part Of: Chemistry. Volume 28:Issue 27(2022)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2022-04-12
• Subjects: carbohydrates -- lectins -- multivalency -- photochemistry -- proteins; Chemistry -- Periodicals; 540
• DOI: 10.1002/chem.202201064
• Languages: English
• ISSNs: 0947-6539

Abstract

Abstract : Photochemical cis – trans isomerization was used to switch a divalent lectin ligand between its two forms, which show contrasting binding properties to the plant lectin wheat germ agglutinin (WGA), as visualized by the yin‐yang symbol. Whereas the E isomer (obtained under irradiation with green light) is able to bridge adjacent binding sites of WGA leading to a high‐affinity chelating binding mode, the Z isomer (obtained under UV light irradiation) crosslinks two lectin molecules associated with a much lower binding affinity. More information can be found in the Research Article by V. Wittmann and co‐authors (DOI: 10.1002/chem.202200267 ).