Journal archive > 2012 > N 1 January-February

STRUCTURAL AND FUNCTIONAL BASES OF THE INTERMOLECULAR INTERACTION
OF CALIX[4]ARENE C-97 WITH MYOSIN SUBFRAGMENT-1 OF MYOMETRIUM

R. D. Labyntseva1, A. A. Bevza1, О. V. Bevza1, S. O. Cherenok2, V. I. Kalchenko2, S. O. Kosterin1

1Palladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Kyiv;
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2Institute of Organic Chemistry, National Academy of Sciences of Ukraine, Kyiv;
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Calix[4]arene C-97 (code is shown) is the macrocyclic compound which has  lipophilic intramolecular higly-structured cavity formed by four aromatic cycles, one of which on the upper rim is modified by methylene bisphosphonic group. It was shown that calix[4]arene C-97 (100 µM) efficiently inhibits ATPase activity of myosin subfragment-1 from pig myometrium, the inhibition coefficient І0.5 being 83 ± 7 µM. At the same time, this compound at 100 µM concentration significantly increases the effective hydrodynamic diameter of myosin subfragment-1, that may be indicative of intermolecular complexation between the calix[4]-arene and myosin head. Computer simulation methods (docking, molecular dynamics, involving the Grid) have been used to clarify structural basis of the intermolecular interaction of calix[4]arene C-97 with myosin subfragment-1 of the myometrium; participation of hydrophobic, electrostatic and ?-? (stacking) interactions between calix[4]arene C-97 and amino acid residues of myosin subfragment-1, some of them being located near the active site of the ATP­ase has been found out.

Key words: ATPase, myosin subfragment-1, calix[4]arene C-97, smooth muscle, uterus­.

The original article in Ukrainian is available for download in PDF format.

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