Tubulin binding, protein-bound conformation in solution, and antimitotic cellular profiling of noscapine and its derivatives.
J Med Chem
; 55(5): 1920-5, 2012 Mar 08.
Article
en En
| MEDLINE
| ID: mdl-22320354
ABSTRACT
Noscapine and its 7-hydroxy and 7-amino derivatives were characterized for their binding to tubulin. A solution NMR structure of these compounds bound to tubulin shows that noscapine and its 7-aniline derivative do not compete for the same binding site nor does its small molecule crystal structure match its tubulin-bound conformation. These compounds were also tested for their antiproliferative effects on a panel hepatocellular carcinoma cell lines.
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Tubulina (Proteína)
/
Moduladores de Tubulina
/
Compuestos de Anilina
/
Antineoplásicos
/
Noscapina
Límite:
Humans
Idioma:
En
Año:
2012
Tipo del documento:
Article