Interaction of 3-acetyl-4-oxo-6,7-dihydro-12H indolo-[2,3-a] quinolizine (AODIQ), a biologically active molecule, with model transport proteins, bovine serum albumin (BSA) and human serum albumin (HSA) have been studied using steady state and picosecond time-resolved fluorescence and fluorescence anisotropy. The polarity dependent intramolecular charge transfer (ICT) process is responsible for the remarkable sensitivity of this biological fluorophore to the protein environments. The CT fluorescence exhibits appreciable hypsochromic shift along with an enhancement in the fluorescence yield, fluorescence anisotropy (r) and fluorescence lifetime upon binding with the proteins. The reduction in the rate of ICT within the hydrophobic interior of albumins leads to an increase in the fluorescence yield and lifetime. Marked increase in the fluorescence anisotropy indicates that the probe molecule is located in a motionally constrained environment within the proteins. Micropolarities in the two proteinous environments have been determined following the polarity sensitivity of the CT emission. Addition of urea to the protein-bound systems leads to a reduction in the fluorescence anisotropy indicating the denaturation of the proteins. Polarity measurements and fluorescence resonance energy transfer (FRET) studies throw light in assessing the location of the fluorophore within the two proteinous media.