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Cover Picture: Calix[ n ]arene‐Based Glycoclusters: Bioactivity of Thiourea‐Linked Galactose/Lactose Moieties as Inhibitors of Binding of Medically Relevant Lectins to a Glycoprotein and Cell‐Surface Glycoconjugates and Selectivity among Human Adhesion/Growth‐Regulatory Galectins (ChemBioChem 10/2008)
Author(s) -
André Sabine,
Sansone Francesco,
Kaltner Herbert,
Casnati Alessandro,
Kopitz Jürgen,
Gabius HansJoachim,
Ungaro Rocco
Publication year - 2008
Publication title -
chembiochem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200890036
Subject(s) - glycoconjugate , lectin , chemistry , ricin , galactose , stereochemistry , glycoprotein , binding selectivity , biochemistry , toxin
The cover picture shows how distinct glycoclusters can interfere with the activity of human adhesion/growth‐regulatory proteins. The three human lectins of medical relevance (Gal‐1, Gal‐3 and Gal‐4) selectively bind to multivalent calixarene glycoconjugates, neutralizing lectin activity. Of note is that the sugar ligands are presented with different spatial topology. This diversity is depicted as generated from an ancient Calix , the etymological origin of the name of these macrocycles. The orange ellipses on the cell surface and on the macrocycle scaffolds (in blue) represent sugar units that compete for lectin binding. In vitro bioassays indicate clear intergalectin selectivity of inhibition that depends on the conformational properties of the calix[ n ]arene scaffold and on the valency of the glycoclusters. The assays also reveal the potent reactivity of the glycoclusters towards a plant toxin from Viscum album L. , akin to ricin. Further details can be found in the article by H.‐J. Gabius, R. Ungaro, et al. on p. 1649 ff.