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Switching of Bacterial Adhesion to a Glycosylated Surface by Reversible Reorientation of the Carbohydrate Ligand
Author(s) -
Weber Theresa,
Chandrasekaran Vijayanand,
Stamer Insa,
Thygesen Mikkel B.,
Terfort Andreas,
Lindhorst Thisbe K.
Publication year - 2014
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201409808
Subject(s) - glycoconjugate , ligand (biochemistry) , chemistry , azobenzene , carbohydrate , glycobiology , adhesion , glycocalyx , epitope , lectin , biophysics , biochemistry , glycoprotein , receptor , biology , molecule , glycan , genetics , antigen , organic chemistry
The surface recognition in many biological systems is guided by the interaction of carbohydrate‐specific proteins (lectins) with carbohydrate epitopes (ligands) located within the unordered glycoconjugate layer (glycocalyx) of cells. Thus, for recognition, the respective ligand has to reorient for a successful matching event. Herein, we present for the first time a model system, in which only the orientation of the ligand is altered in a controlled manner without changing the recognition quality of the ligand itself. The key for this orientational control is the embedding into an interfacial system and the use of a photoswitchable mechanical joint, such as azobenzene.