Abstract
This paper vividly indicates that steady state as well as time-resolved fluorescence techniques can serve as highly sensitive monitors to explore the interactions of 5,7-dimethoxy-2,3,4,9-tetrahydro-1H-carbazol-1-one with model transport proteins, bovine serum albumin (BSA) and human serum albumin (HSA). Besides these, we have used fluorescence anisotropy study to assess the degree of restrictions imparted by the micro-environments of serum albumins. Again, to speculate the triplet excited state interaction between such fluorophore and albumin proteins (BSA& HSA), laser flash-photolysis experiments have been carried out. Molecular docking experiments have also been performed to support the conclusions obtained from steady state experiments.
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Acknowledgements
This work has been funded by Chemical and Biophysical Approaches for Understanding of Natural Processes (CBAUNP) project, SINP of the Department of Atomic Energy (DAE), Government of India. Thanks to CSIR, New Delhi for providing financial help in the form of fellowships. Special thanks to Mr. Amartya Krishna Mitra for being a constant source of inspiration. We also want to thank Mrs. Sayantani Mitra for her sincere support in perusing the paper and making suitable modifications in language.
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Mitra, A.K., Sau, A., Pal, U. et al. Constrained Photophysics of 5,7-dimethoxy-2,3,4,9-tetrahydro-1H-carbazol-1-one in the Bioenvironment of Serum Albumins: A Spectroscopic Endeavour Supported by Molecular Docking Analysis. J Fluoresc 27, 1547–1558 (2017). https://doi.org/10.1007/s10895-017-2094-2
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DOI: https://doi.org/10.1007/s10895-017-2094-2