| Autor: |
Eguchi, Masakatsu, McMillan, Michael, Nguyen, Cu, Teo, Jia-Ling, Chi, Emil, Henderson Jr., William, Kahn, Michael |
| Zdroj: |
Combinatorial Chemistry & High Throughput Screening; November 2003, Vol. 6 Issue: 7 p611-621, 11p |
| Abstrakt: |
There is increasing evidence that redox regulation of transcription, particularly activator protein-1 (AP-1) and nuclear factor kappa B (NF-kB), is important in inflammatory diseases. Human thioredoxin (TRX), a member of the oxidoreductase superfamily, was initially identified, as a factor which augments the production of interleukin-2 receptor alpha (IL-2R ) in human T-cell lymphotropic virus type 1 (HTLV-1) infected patient T-cells. Substrates for the redox activity of TRX bind the active site cleft in extended strand structure. The rapid generation of high numbers of peptide secondary structure mimetics through solid-phase synthesis is a key technology for the identification of pharmaceutical leads based on such protein-peptide interactions. In this manuscript, we describe a chemogenomic approach utilizing an extended strand templated library to develop small molecule inhibitors to validate oxidoreductase molecular targets in a murine asthma model. |
| Databáze: |
Supplemental Index |
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