Journal
JOURNAL OF MEDICINAL CHEMISTRY
Volume 56, Issue 4, Pages 1509-1519Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jm301221x
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Funding
- International Graduate School of Science and Engineering (IGSSE)
- TUM Graduate School (TUM GS)
- Max Planck Society
- European Union [NMP4-LA-2009-229289 NanoII, NMP3-SL-2009-229294 NanoCARD]
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Integrins are the major class of cell adhesion proteins. Their interaction with different ligands of the extracellular matrix is diverse. To get more insight into these interactions, artificial ligands endowed with a well-defined activity/selectivity profile are necessary. Herein, we present a library of cyclic pentapeptides, based on our previously reported peptide motif c(-phg-isoDGR-X-), in which high activity toward fibronectin binding integrins alpha 5 beta 1 and alpha v beta 6 and not on vitronectin binding integrins alpha v beta 3 and alpha v beta 5 has been achieved by changing the flanking amino acids. The structure of the most promising candidates has been determined using a combined approach of NMR, distance geometry, and molecular dynamics simulations, and docking studies have been further used to elucidate the peptide-integrin interactions at the molecular level. The peptides' binding affinity has been characterized by enzyme linked immunosorbent assay experiments, and the results have been verified by cell adhesion experiments on specifically functionalized surfaces.
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