Calix[4]arene C-90 and its analogs activate ATPase of the myometrium myosin subfragment-1.
Ukr Biochem J
; 88(5): 48-61, 2016.
Article
en En
| MEDLINE
| ID: mdl-29235801
Numerous female reproductive abnormalities are consequences of disorders in uterus smooth muscle (myometrium) contractile function. In this work, we described activators of ATPase, which could be used for development of effective treatments for correcting this dysfunction. Myosin ATPase localized in the catalytic domain of myosin subfragment-1 transforms a chemical energy deposited in macroergic bonds of ATP into mechanical movement. It was shown that Ñalix[4]arene C-90 and its structural analogs functionalized at the upper rim of macrocycle with four or at least two N-phenylsulfonÑltrifluoroacetamidine groups, are able to activate ATP hydrolysis catalyzed by myometrium myosin subfragment-1. It was shown with the method of computer modeling that N-phenylsulfonÑltrifluoroacetamidine groups of calix[4]arene C-90 interact with responsible for binding, coordination and the hydrolysis of ATP amino acid residues of myosin subfragment-1. The results can be used for further research aimed at using calix[4]arene C-90 and its analogs as pharmacological compounds that can effectively normalize myometrium contractile hypofunction.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Fenoles
/
Adenosina Trifosfato
/
Miosinas
/
Subfragmentos de Miosina
/
Calixarenos
/
Miometrio
Límite:
Animals
Idioma:
En
Revista:
Ukr Biochem J
Año:
2016
Tipo del documento:
Article
Pais de publicación:
Ucrania