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| - Spectroscopic Investigation on the Interaction of ICT Probe 3-Acetyl-4-oxo-6,7-dihydro-12HIndolo-[2,3-a] Quinolizine with Serum Albumins
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| - Interaction of 3-acetyl-4-oxo-6,7-dihydro-12H indolo-[2,3-a] quinolizine (AODIQ), a biologically activemolecule, 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 sensitivityof this biological fluorophore to the protein environments. The CT fluorescence exhibits appreciablehypsochromic shift along with an enhancement in the fluorescence yield, fluorescence anisotropy (r) andfluorescence lifetime upon binding with the proteins. The reduction in the rate of ICT within the hydrophobicinterior of albumins leads to an increase in the fluorescence yield and lifetime. Marked increase in thefluorescence anisotropy indicates that the probe molecule is located in a motionally constrained environmentwithin the proteins. Micropolarities in the two proteinous environments have been determined following thepolarity sensitivity of the CT emission. Addition of urea to the protein-bound systems leads to a reduction inthe fluorescence anisotropy indicating the denaturation of the proteins. Polarity measurements and fluorescenceresonance energy transfer (FRET) studies throw light in assessing the location of the fluorophore within thetwo proteinous media.
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