Molecular tongs containing amino acid mimetic fragments: new inhibitors of wild-type and mutated HIV-1 protease dimerization.
J Med Chem
; 49(15): 4657-64, 2006 Jul 27.
Article
en En
| MEDLINE
| ID: mdl-16854071
ABSTRACT
We have designed, synthesized, and evaluated the inhibitory activity and metabolic stability of new peptidomimetic molecular tongs based on a naphthalene scaffold for inhibiting HIV-1 protease dimerization. Peptidomimetic motifs were inserted into one peptidic strand to make it resistant to proteolysis. The peptidic character of the molecular tongs can be decreased without changing the way they inhibit dimerization. Mutated HIV-1 proteases are also vulnerable to dimerization inhibitors, and the multimutated protease ANAM-11 is twice as sensitive to the inhibitor compared to wild-type protease. Thus, the metabolic stability of antidimeric molecular tongs can be increased without compromising their ability to inhibit wild-type and mutated HIV-1 proteases in vitro.
Buscar en Google
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Proteasa del VIH
/
Inhibidores de la Proteasa del VIH
/
Aminoácidos
Idioma:
En
Revista:
J Med Chem
Asunto de la revista:
QUIMICA
Año:
2006
Tipo del documento:
Article
País de afiliación:
Francia