- Tytuł:
- ATP-binding domain of NTPase/helicase as a target for hepatitis C antiviral therapy.
- Autorzy:
-
Borowski, Peter
Mueller, Oliver
Niebuhr, Andreas
Kalitzky, Matthias
Hwang, Lih-Hwa
Schmitz, Herbert
Siwecka, Maria
Kulikowski, Tadeusz - Powiązania:
- https://bibliotekanauki.pl/articles/1044428.pdf
- Data publikacji:
- 2000
- Wydawca:
- Polskie Towarzystwo Biochemiczne
- Tematy:
-
ribavirin-5'-triphosphate
enzyme inhibition
HCV NTPase/helicase - Opis:
- To enhance the inhibitory potential of 1-β-D-ribofuranosyl-1,2,4-triazole-3-carboxamide (ribavirin) vs hepatitis C virus (HCV) NTPase/helicase, ribavirin-5'-triphosphate (ribavirin-TP) was synthesized and investigated. Ribavirin-TP was prepared with the use of modified Yoshikawa-Ludwig-Mishra-Broom procedure (cf. Mishra & Broom, 1991, J. Chem. Soc., Chem. Commun, 1276-1277) involving phosphorylation of unprotected nucleoside. Kinetic analysis revealed enhanced inhibitory potential of ribavirin-TP (IC50=40 μM) as compared to ribavirin (IC50 > 500 μM). Analysis of the inhibition type by means of graphical methods showed a competitive type of inhibition with respect to ATP. In view of the relatively low specificity towards nucleoside-5'-triphosphates (NTP) of the viral NTPase/helicases, it could not be ruled out that the investigated enzyme hydrolyzed the ribavirin-TP to less potent products. Investigations on non- hydrolysable analogs of ribavirin-TP or ribavirin-5'-diphosphate (ribavirin-DP) are currently under way.
- Źródło:
-
Acta Biochimica Polonica; 2000, 47, 1; 173-180
0001-527X - Pojawia się w:
- Acta Biochimica Polonica
- Dostawca treści:
- Biblioteka Nauki
Artykuł