Photoswitching Affinity and Mechanism of Multivalent Lectin Ligands

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OSSWALD, Uwe, Johannes BONEBERG, Valentin WITTMANN, 2022. Photoswitching Affinity and Mechanism of Multivalent Lectin Ligands. In: Chemistry - A European Journal. Wiley. 28(27), e202200267. ISSN 0947-6539. eISSN 1521-3765. Available under: doi: 10.1002/chem.202200267

@article{Osswald2022-05-11Photo-57051, title={Photoswitching Affinity and Mechanism of Multivalent Lectin Ligands}, year={2022}, doi={10.1002/chem.202200267}, number={27}, volume={28}, issn={0947-6539}, journal={Chemistry - A European Journal}, author={Osswald, Uwe and Boneberg, Johannes and Wittmann, Valentin}, note={Article Number: e202200267} }

<rdf:RDF xmlns:dcterms="" xmlns:dc="" xmlns:rdf="" xmlns:bibo="" xmlns:dspace="" xmlns:foaf="" xmlns:void="" xmlns:xsd="" > <rdf:Description rdf:about=""> <dc:contributor>Osswald, Uwe</dc:contributor> <dc:language>eng</dc:language> <dcterms:abstract xml:lang="eng">Multivalent receptor-ligand binding is a key principle in a plethora of biological recognition processes. Immense binding affinities can be achieved with the correct spatial orientation of the ligands. Accordingly, the incorporation of photoswitches, that can be used to reversibly change the spatial orientation of molecules, into multivalent ligands is a means to alter the binding affinity and possibly also the binding mode of such ligands. We report a divalent ligand for the model lectin wheat germ agglutinin (WGA) containing an arylazopyrazole photoswitch. This switch, that has been recently introduced as an alternative to the more commonly used azobenzene moiety, is characterized by almost quantitative E / Z photoswitching in both directions, high quantum yields, and high thermal stability of the Z isomer. The ligand was designed in a way that only one of the isomers is able to bridge adjacent binding sites of WGA leading to a chelating binding mode. Photoswitching induces an unprecedentedly high change in lectin binding affinity as determined by isothermal titration calorimetry (ITC). Furthermore, additional dynamic light scattering (DLS) data suggest that the binding mode of the ligand changes from chelating binding of the E isomer to crosslinking binding of the Z isomer.</dcterms:abstract> <dc:creator>Wittmann, Valentin</dc:creator> <dc:date rdf:datatype="">2022-03-29T12:27:44Z</dc:date> <dspace:isPartOfCollection rdf:resource=""/> <foaf:homepage rdf:resource="http://localhost:8080/jspui"/> <dc:creator>Osswald, Uwe</dc:creator> <dspace:isPartOfCollection rdf:resource=""/> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dspace:hasBitstream rdf:resource=""/> <dcterms:isPartOf rdf:resource=""/> <dc:contributor>Boneberg, Johannes</dc:contributor> <dc:creator>Boneberg, Johannes</dc:creator> <dcterms:title>Photoswitching Affinity and Mechanism of Multivalent Lectin Ligands</dcterms:title> <dcterms:available rdf:datatype="">2022-03-29T12:27:44Z</dcterms:available> <dcterms:issued>2022-05-11</dcterms:issued> <dcterms:hasPart rdf:resource=""/> <bibo:uri rdf:resource=""/> <dc:rights>terms-of-use</dc:rights> <dc:contributor>Wittmann, Valentin</dc:contributor> <dcterms:rights rdf:resource=""/> <dcterms:isPartOf rdf:resource=""/> </rdf:Description> </rdf:RDF>

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