Structure based development of novel specific inhibitors for cathepsin L and cathepsin S in vitro and in vivo.
FEBS Lett
; 458(1): 6-10, 1999 Sep 10.
Article
en En
| MEDLINE
| ID: mdl-10518923
ABSTRACT
Specific inhibitors for cathepsin L and cathepsin S have been developed with the help of computer-graphic modeling based on the stereo-structure. The common fragment, N-(L-trans-carbamoyloxyrane-2-carbonyl)-phenylalanine-dimethyla mide, is required for specific inhibition of cathepsin L. Seven novel inhibitors of the cathepsin L inhibitor Katunuma (CLIK) specifically inhibited cathepsin L at a concentration of 10(-7) M in vitro, while almost no inhibition of cathepsins B, C, S and K was observed. Four of the CLIKs are stable, and showed highly selective inhibition for hepatic cathepsin L in vivo. One of the CLIK inhibitors contains an aldehyde group, and specifically inhibits cathepsin S at 10(-7) M in vitro.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Endopeptidasas
/
Fenilalanina
/
Carbamatos
/
Catepsinas
/
Leucina
Tipo de estudio:
Prognostic_studies
Límite:
Animals
/
Humans
Idioma:
En
Revista:
FEBS Lett
Año:
1999
Tipo del documento:
Article
País de afiliación:
Japón