Spectroscopic study of interaction of styrylcyanine dye Sbt and its derivatives with bovine serum albumin

The spectral-fluorescent characteristics of styrylcyanine dye Sbt ((E)-2-(4-(dimethylamino) styryl)-3-methylbenzod]thiazol-3-ium iodide) and homodimers, dyes conjugated with two chromophores in aqueous solutions without and in the presence of bovine serum albumin (BSA), are studied. It is established that in the presence of BSA for dyes Dbt-5 and Dbt-10, an increase of the absorptivity, a slight broadening and the emergence of new band on the short wavelength range with λ_max=410 nm is observed; also hypsochromic shift of the absorption and fluorescence at 30 nm and 7 nm, respectively for the dye D-183 is observed. The intensity of the fluorescence emission fundamental band in all the studied dyes in the presence of BSA increases by 3.5 to 55 times. The binding constant (K) and number of binding sites (N) of studied dyes with BSA are determined. The dependence of the binding constants with BSA from the dipole moment of dye molecules is identified, which shows that in addition to the electrostatic attraction forces between molecules of styrylcyanine dyes with BSA, hydrophobic interactions are essential. It is shown that the aggregation of dye affects the processes of interaction of the dyes with the BSA.