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Cover Feature: Photoswitching Affinity and Mechanism of Multivalent Lectin Ligands (Chem. Eur. J. 27/2022)
Author(s) -
Osswald Uwe,
Boneberg Johannes,
Wittmann Valentin
Publication year - 2022
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.202201064
Subject(s) - lectin , chemistry , wheat germ agglutinin , isomerization , soybean agglutinin , photoisomerization , divalent , ligand (biochemistry) , stereochemistry , molecule , biophysics , receptor , biochemistry , biology , catalysis , organic chemistry
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).