Non-peptide inhibitors of HCV serine proteinase.
FEBS Lett
; 421(3): 217-20, 1998 Jan 16.
Article
en En
| MEDLINE
| ID: mdl-9468309
ABSTRACT
We screened a chemical library of 2000 compounds for inhibitors of hepatitis C virus (HCV) serine proteinase using an in vitro screening method measuring the hydrolysis of the peptide substrate. Three compounds were found to be the most potent inhibitors (IC50 < 10(-5) M). Two of them had a similar structure, that of halogenated benzanilide, and were not inhibitory for common serine proteinases. They inhibited the enzyme non-competitively with the substrate. Together with the result of the analogous compounds in the chemical library, the presumed structural requirements of the inhibition are pointed out.
Buscar en Google
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Serina Endopeptidasas
/
Inhibidores de Serina Proteinasa
/
Proteínas no Estructurales Virales
Límite:
Humans
Idioma:
En
Revista:
FEBS Lett
Año:
1998
Tipo del documento:
Article
País de afiliación:
Japón