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 subfragment1 (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. The conformational changes in myosin active site due to ATP hydrolysis are enhanced with the assis tance of switch 1, switch 2, relay and converter and transferred to the regulatory domain -lever arm, which plays an essential role in the generation of force and movement [13]. As a result, myosin moves along the actin filament causing the muscle contrac tion. That is why myosin catalyzed ATP hydrolysis is considered as one of the most important processes in the molecular mechanism of the myometrium con traction.The known pathologies of uterus contractile function (weak labor contraction, preterm birth, miscarriage, atony, hypo and hypertonicity of the uterus, etc.) occur due to the uterine smooth mus cle contractionrelaxation dysfunction [4].Therefore, it is vital to develop new effective pharmacological substances capable of normalizing uterine func tion. The molecular basis for designing potentially bioactive compounds could be calix [4]arenes -syn thetic macrocyclic phenol oligomers, which have a cupshaped structure with various (by their chemi cal nature) substituents at the upper and lower rims. 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 develo ping new effective drugs [5,6].Calix [4]arenes are able to modify the functional activity of certain proteins, particularly the activity of enzymes. We have previously shown that calix[4]a