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Cover Picture: STD and trNOESY NMR Study of Receptor–Ligand Interactions in Living Cancer Cells (ChemBioChem 5/2011)
Author(s) -
Potenza Donatella,
Vasile Francesca,
Belvisi Laura,
Civera Monica,
Araldi Elena M. V.
Publication year - 2011
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.201190015
Subject(s) - chemistry , ligand (biochemistry) , nuclear magnetic resonance spectroscopy , integrin , docking (animal) , stereochemistry , biophysics , receptor , biochemistry , biology , medicine , nursing
The cover picture shows a schematic NMR tube in which our cyclic RGD mimic (targeting integrin α v β 3 ) interacts with a suspension of intact bladder cancer cells. The integrin α v β 3 overexpressed on the cell membrane is labelled in red. The interaction between small ligands and membrane‐bound proteins can be observed by NMR techniques directly on living cells, without the need to isolate the protein receptor. The saturation transfer difference (STD) spectrum, shown on the right, identifies the epitope of the mimic. The insight provided by NMR spectroscopy is completed by docking calculations, thus defining the ligand's integrin‐bound conformation and the ligand–receptor interactions at a molecular level. The binding mode of our RGD mimic into the crystal structure of the α v β 3 integrin is shown at the bottom. For further information, see the communication by D. Potenza et al. on p. 695 ff.