Calix[4]arene C-90 and its analogs activate ATPase of the myometrium myosin subfragment-1

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...

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Main Authors: R. D. Labyntseva, O. V. Bevza, K. V. Lytvyn, M. O. Borovyk, R. V. Rodik, V. I. Kalchenko, S. O. Kosterin
Format: Article
Language:English
Published: National Academy of Sciences of Ukraine, Palladin Institute of Biochemistry 2016-10-01
Series:The Ukrainian Biochemical Journal
Subjects:
Online Access:http://ukrbiochemjournal.org/wp-content/uploads/2016/11/Labyntseva_5_16.pdf
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author R. D. Labyntseva
O. V. Bevza
K. V. Lytvyn
M. O. Borovyk
R. V. Rodik
V. I. Kalchenko
S. O. Kosterin
author_facet R. D. Labyntseva
O. V. Bevza
K. V. Lytvyn
M. O. Borovyk
R. V. Rodik
V. I. Kalchenko
S. O. Kosterin
author_sort R. D. Labyntseva
collection DOAJ
description 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.
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spelling doaj.art-3f2d7bf8224d40a0a4c1f6ff40a900d12023-12-02T14:35:57ZengNational Academy of Sciences of Ukraine, Palladin Institute of BiochemistryThe Ukrainian Biochemical Journal2409-49432413-50032016-10-01885486110.15407/ubj88.05.048Calix[4]arene C-90 and its analogs activate ATPase of the myometrium myosin subfragment-1R. D. Labyntseva0O. V. Bevza1 K. V. Lytvyn2M. O. Borovyk3R. V. Rodik4V. I. Kalchenko5 S. O. Kosterin6Palladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Kyiv;Palladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Kyiv;Palladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Kyiv;2Institute of Organic Chemistry, National Academy of Sciences of Ukraine, Kyiv2Institute of Organic Chemistry, National Academy of Sciences of Ukraine, KyivInstitute of Organic Chemistry, National Academy of Sciences of Ukraine, KyivPalladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Kyiv;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.http://ukrbiochemjournal.org/wp-content/uploads/2016/11/Labyntseva_5_16.pdfATPase activitycalix[4]arene C-90dockingmyometrium smooth musclesmyosin subfragment-1
spellingShingle R. D. Labyntseva
O. V. Bevza
K. V. Lytvyn
M. O. Borovyk
R. V. Rodik
V. I. Kalchenko
S. O. Kosterin
Calix[4]arene C-90 and its analogs activate ATPase of the myometrium myosin subfragment-1
The Ukrainian Biochemical Journal
ATPase activity
calix[4]arene C-90
docking
myometrium smooth muscles
myosin subfragment-1
title Calix[4]arene C-90 and its analogs activate ATPase of the myometrium myosin subfragment-1
title_full Calix[4]arene C-90 and its analogs activate ATPase of the myometrium myosin subfragment-1
title_fullStr Calix[4]arene C-90 and its analogs activate ATPase of the myometrium myosin subfragment-1
title_full_unstemmed Calix[4]arene C-90 and its analogs activate ATPase of the myometrium myosin subfragment-1
title_short Calix[4]arene C-90 and its analogs activate ATPase of the myometrium myosin subfragment-1
title_sort calix 4 arene c 90 and its analogs activate atpase of the myometrium myosin subfragment 1
topic ATPase activity
calix[4]arene C-90
docking
myometrium smooth muscles
myosin subfragment-1
url http://ukrbiochemjournal.org/wp-content/uploads/2016/11/Labyntseva_5_16.pdf
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AT moborovyk calix4arenec90anditsanalogsactivateatpaseofthemyometriummyosinsubfragment1
AT rvrodik calix4arenec90anditsanalogsactivateatpaseofthemyometriummyosinsubfragment1
AT vikalchenko calix4arenec90anditsanalogsactivateatpaseofthemyometriummyosinsubfragment1
AT sokosterin calix4arenec90anditsanalogsactivateatpaseofthemyometriummyosinsubfragment1