New C25 carbamate rifamycin derivatives are resistant to inactivation by ADP-ribosyl transferases.
Bioorg Med Chem Lett
; 17(2): 522-6, 2007 Jan 15.
Article
em En
| MEDLINE
| ID: mdl-17070048
ABSTRACT
A novel series of 3-morpholino rifamycins in which the C25 acetate group was replaced by a carbamate group were prepared and found to exhibit significantly improved antimicrobial activity than rifampin against Mycobacterium smegmatis. Further characterization of such compounds suggests that relatively large groups attached to the rifamycin core via a C25 carbamate linkage prevent inactivation via ribosylation of the C23 alcohol as catalyzed by the endogenous rifampin ADP-ribosyl transferase of M. smegmatis. SAR studies of the C25 carbamate rifamycin series against M. smegmatis and other bacteria are reported.
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Base de dados:
MEDLINE
Assunto principal:
Rifamicinas
/
ADP Ribose Transferases
/
Antibacterianos
Idioma:
En
Ano de publicação:
2007
Tipo de documento:
Article