Fluorometric investigation of interaction of 3-acetyl-4-oxo-6,7-dihydro-12H indolo-[2,3-a] quinolizine with bovine serum albumin.

Interaction of 3-acetyl-4-oxo-6,7-dihydro-12H indolo-[2,3-a] quinolizine (AODIQ) with a model transport protein, bovine serum albumin (BSA), has been studied using steady state fluorescence and fluorescence anisotropy experiments. Upon binding with BSA, the charge transfer (CT) fluorescence exhibits appreciable hypsochromic shift along with an enhancement in the fluorescence intensity. Gradual addition of BSA leads to the marked increase in the fluorescence anisotropy (r). From the high value of fluorescence anisotropy (r=0.30) it is argued that the probe molecule is located in motionally restricted environment of the protein. Addition of urea to the protein bound AODIQ leads to the decrease in fluorescence intensity as well as fluorescence anisotropy (r) indicating the release of AODIQ molecule to the aqueous buffer medium, thus supporting the idea that the protein, in its native form, binds with the probe. The binding constant and free energy change (DeltaG(0)) for the interaction of AODIQ with BSA have been evaluated from relevant fluorescence data. Polarity of the microenvironment has been determined from a comparison of the variation of fluorescence property of the probe in dioxane-water mixture with varying composition.