甾体化合物与钠钾依赖型ATP酶“洋地黄”受体位点相互作用的结构基础。

Structural basis of steroid compounds interaction with "digitalis"-receptor sites of Na,K-dependent ATPase.

作者信息

Kamernitzky A V, Reshetova I G, Ovchinnikov A A, Shamovsky I L, Massova I A, Mirsalikhova N M

机构信息

N. D. Zelinsky Institute of Organic Chemistry of the USSR Academy of Sciences, Moscow.

出版信息

J Steroid Biochem. 1989 Jun;32(6):857-63. doi: 10.1016/0022-4731(89)90464-0.

DOI:10.1016/0022-4731(89)90464-0

PMID:2547115

Abstract

Twenty-two Steroid molecules have been tested for the inhibition Na,K-dependent ATPase at 10(-7)-10(-4) M concentrations. At the 10(-5) M concentration of the investigated molecules, inhibition ranged from 8 to 36%. To explain the structure-inhibition % relationship, we determined the value of heteropolarity or biphilicity moment of these molecules. This value would appear to be dependent on the space location and hydrophilicity of the molecule elementary fragments, and to the degree of their water accessibility; however, it is independent of the hydrophilicity of the molecules as a whole. On the basis of the obtained data, details of Na,K-ATPase digitalis-receptor structure and the mechanism of the glycoside-receptor interaction are discussed.

摘要

已对22种甾体分子在10⁻⁷ - 10⁻⁴ M浓度下抑制钠钾依赖型ATP酶的能力进行了测试。在所研究分子的10⁻⁵ M浓度下，抑制率范围为8%至36%。为了解释结构与抑制率%之间的关系，我们测定了这些分子的异极性或双亲性矩值。该值似乎取决于分子基本片段的空间位置和亲水性，以及它们的水可及程度；然而，它与整个分子的亲水性无关。根据所获得的数据，讨论了钠钾ATP酶洋地黄受体结构的细节以及糖苷-受体相互作用的机制。