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Cover Picture: Rational Design of Highly Active and Selective Ligands for the α5β1 Integrin Receptor (ChemBioChem 9/2008)
Author(s) -
Heckmann Dominik,
Meyer Axel,
Laufer Burkhardt,
Zahn Grit,
Stragies Roland,
Kessler Horst
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.200890032
Subject(s) - integrin , rational design , chemistry , receptor , angiogenesis , cover (algebra) , biophysics , computational biology , stereochemistry , biochemistry , biology , nanotechnology , cancer research , materials science , engineering , mechanical engineering
The cover picture shows the Conolly surface of the X‐ray structure of the integrin αvβ3 and the homology model of the related integrin α5β1. The spatial differences between both integrins have been used to develop biased compound libraries that yield high‐affinity ligands which bind to α5β1 in the range of 1 n M but have very low affinity for αvβ3. Both integrins are involved in angiogenesis but their individual role is still under debate. The ligands described here allow us to study the biological roles of both integrins and might additionally serve as potential drug candidates to target selectively the α5β1 integrin in the antiangiogenic therapy of cancer and age‐related macular degeneration. For further information, see the article by H. Kessler et al. on p. 1397 ff.