Abstract
The generation of drugs that modulate the activities of particular protein kinases has become a prime focus of the pharmaceutical and biotechnology industry. Consequently, improved methods for the development of high-throughput screening formats for these enzymes is a high priority. In the present study, we have designed three generic peptide substrates that can be used to assay a diverse range of protein kinases. These peptides share a common seven-residue epitope that includes the site of phosphorylation, and against which we have generated a phospho-specific antibody. Thus a large number of serine/threonine-specific protein kinases can be screened using a simple non-radioactive format.
| Original language | English |
|---|---|
| Pages (from-to) | 977-981 |
| Number of pages | 5 |
| Journal | Biochemical Journal |
| Volume | 366 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - 15 Sept 2002 |
Keywords
- Drug discovery
- High-throughput screening
- Peptide substrate
- Phospho-specific antibody
- Protein kinase inhibitor
ASJC Scopus subject areas
- Biochemistry