Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1372147 | Bioorganic & Medicinal Chemistry Letters | 2011 | 4 Pages |
Abstract
Protein kinases are widely recognized as important therapeutic targets due to their involvement in signal transduction pathways. These pathways are tightly controlled and regulated, notably by the ability of kinases to selectively phosphorylate a defined set of substrates. As part of a study on the substrate requirements of Insulin-like Growth Factor 1 Receptor (IGF-1R) and Insulin Receptor (InsR), we evaluated and applied a universal assay system able to monitor the phosphorylation of unlabelled peptides of any length in real time. In contrast to already reported profiling methodologies, we were able to assess the kcat/KM ratio of peptides as short as tetramers. Notably, we were able to identify an efficient pentamer substrate that exhibited kinetic properties close to those of a 250-amino acid protein derived from IRS-1, a natural substrate of IGF-1R and InsR.
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Organic Chemistry
Authors
Julien Chapelat, Frédéric Berst, Andreas L. Marzinzik, Henrik Moebitz, Peter Drueckes, Doriano Fabbro, Joerg Trappe, Dieter Seebach,