Interaction mechanism of anabolic steroid hormones with structural components of erythrocyte membranes.

The interaction of testosterone, androsterone, dehydroepiandrosterone (DHEA), and dehydroepiandrosterone sulfate (DHEAS) with erythrocyte membranes was studied. It was shown that testosterone and androsterone have a high constant of binding to the membranes (K(b) ≈ 10(6) M(-1)), whereas K(b)'s for DHEA and DHEAS are 2 orders of magnitude lower. Hydrogen bonds and hydrophobic interactions play an important role in binding of anabolic steroids.

Interaction mechanism of cortisol and catecholamines with structural components of erythrocyte membranes.

Nonspecific mechanisms of the stress hormones interaction with erythrocyte membranes were studied by means of atomic force microscopy, fluorescence analysis, and IR spectroscopy. It was shown that stress hormones (cortisol, adrenaline, noradrenaline) can bind to erythrocyte membranes with high affinity (K(b) approximately 10(6) M(-1)). The binding mechanism involves hydrogen bonds and hydrophobic and electrostatic interactions.

[Mechanisms of interaction of tetrahydrocortisol and its complex with apolipoprotein A-I and DNA regulatory cis-elements of CC(GCC)5/GG(CGG)5 type].

An IR-spectroscopy study of the mechanism of interaction between duplex CC(GCC)5/GG (CGG)5Li2 and tetrahydrocortisol or tetrahydrocortisol-apolipoprotein A-I complex revealed the formation of hydrogen bonds between the OH group of the tetrahydrocortisol A-ring and the C=0 group of cytosine or guanine. Tetrahydrocortisol forms hydrogen bonds with the PO2-group of the duplex and with the OH-group of monosaccharide. The interaction of tetrahydrocortisol and apolipoprotein A-I with the duplex occurs at the same active site, namely, with the C=O-group of bases.

Changes in the secondary structure of highly polymeric DNA and CC(GCC)n-type oligonucleotides under the action of steroid hormones and their complexes with apolipoprotein A I.

A small-angle X-ray scattering study showed that the action of tetrahydrocortisol (THC) in complex with apolipoprotein A I (ApoA-I) on DNA leads to local melting of DNA. The most probable site of interaction between this complex and DNA is the (GCC)n-type sequence. Oligonucleotides (duplexes) of this type have been synthesized.

[Anomalous change in the specific conductivity in lipoproteins at around physiologic temperatures].

Studying the temperature dependence of conductivity sigma of rat and human lipoproteins and apoprotein A-I fractions revealed an anomalous region in the range of temperatures (35-38) +/- 0.5 degree C. The activation energy delta H and temperature coefficient sigma (delta sigma/delta T) on both sides of Tc and the heat of transition (delta H of transition) were calculated.