| Autor: |
Donkor IO; Department of Pharmaceutical Sciences, University of Tennessee Health Science Center, Memphis, TN 38163, USA. idonkor@utmem.edu, Korukonda R, Huang TL, LeCour L Jr |
| Jazyk: |
angličtina |
| Zdroj: |
Bioorganic & medicinal chemistry letters [Bioorg Med Chem Lett] 2003 Mar 10; Vol. 13 (5), pp. 783-4. |
| DOI: |
10.1016/s0960-894x(03)00021-0 |
| Abstrakt: |
Four new peptidyl aldehydes bearing proline mimetics at the P(2)-position were synthesized and studied as inhibitors of calpain I, cathepsin B, and selected serine proteases. The ring size of the P(2)-constraining residue influenced the inhibitory potency and selectivity of the compounds for calpain I compared to the other proteases. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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