The Interaction Of Homodimer Styrylcyanine Dyes With Sodium Dodecyl Sulfate And Triton X-100.

Solubilization of the styrylcyanine dye Sbt ((E)-2-(4-(dimethylamino)styryl)-3-methylbenzo[d]thiazol-3-ium iodide) and its homodimers Dbt-5 and Dbt-10 in aqueous solution of sodium dodecyl sulfate and Triton X-100 has been studied by steady state and picosecond time-resolved fluorescence spectroscopy. At low concentration of sodium dodecyl sulfate in solution, between Sbt, Dbt-5 dyes molecules and surfactant ion pairs are formed followed by the formation non-luminescent H-aggregates. The nature of the interaction between molecules of dyes and surfactants has been revealed.

Electronic nature and structure of aggregates of riboflavin molecules.

Aggregation process of riboflavin molecules in binary mixtures: water - dioxane, water - DMSO, and ethanol - isobutanol, were investigated using spectroscopic methods and quantum-chemical calculation. It was shown that at a constant concentration of riboflavin and different ratios of binary mixtures, a deformation of the electronic absorption spectra with a hypochromic effect is observed. The observed changes are caused by the formation of a hydrogen bond and dipole-dipole interaction between riboflavin molecules, which is accompanied by a shift and resonance splitting of excited electronic levels.

[Fluorescence of acridine orange in the composition of blood and tissues].

The interaction of acridine orange with blood albumins and tissue cells from different organs of white mouse has been studied by the spectral luminescence method. It was shown that acridine orange, by penetrating cells or orangelles, is able to intercalate between base pairs in the DNA molecule. It was found that the application of acridine orange as a fluorescent probe can influence the metabolic activity of organs.

[A study of blood albumin of various animal species by the spectral luminescent method].

The functional differences of blood serum albumin of some animal species have been studied using the spectral luminescent method by comparing the binding constants K and the concentration of binding sites N of rhodamine B and rhodanmine S to albumin. It was shown that K and N depend on both the concentration of blood serum albumin and animal species and the dye used.