Abstract
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 сalix[4]arene C-90 and its structural analogs functionalized at the upper rim of macrocycle with four or at least two N-phenylsulfonуltrifluoroacetamidine groups, are able to activate ATP hydrolysis catalyzed by myometrium myosin subfragment-1. It was shown with the method of computer modeling that N-phenylsulfonуltrifluoroacetamidine 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.
Highlights
M yometrium contractile function is asso ciated with the activity of the main struc tural and contractile protein of uterus smooth muscle – actomyosin, in which myosin ex hibits enzyme activity, namely the ability to hydro lyze ATP
It was shown that 100 μM calix[4]arene C-90 effectively activated ATP hydrolysis catalyzed by swine myometrium actomyosin [7]
The enzyme activity of actomyosin complex is associated with the operation of the active center of myosin ATPase localized in the catalytic domain of myosin S1
Summary
M yometrium contractile function is asso ciated with the activity of the main struc tural and contractile protein of uterus smooth muscle – actomyosin, in which myosin ex hibits enzyme activity, namely the ability to hydro lyze ATP. Myosin ATPase, localized in the catalytic domain of subfragment-1 (S1 or head), is called a biomolecular motor It uses the free energy of ATP hydrolysis deposited in ATP macroergic bonds for cyclic changes in the structure of the myosin head. Calix[4]arenes formed by four functionalized arene fragments are characterized by rather a flexible macrocycle conformation, low toxicity of the matrix and the ability to penetrate into the cell. All these properties make calix[4]arenes promising agents for developing new effective drugs [5, 6]. Using computer modeling we investigated the mechanisms of action of calix[4]arene C-90 and its analogs on the hydrolytic activity of myosin S1
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