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Molecular spectroscopic and docking analysis of the interaction of fluorescent thiadicarbocyanine dye with biomolecule bovine serum albumin

Katrahalli, U and Shanker, G and Pal, D and Hadagali, MD (2022) Molecular spectroscopic and docking analysis of the interaction of fluorescent thiadicarbocyanine dye with biomolecule bovine serum albumin. In: Journal of Biomolecular Structure and Dynamics .

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Official URL: https://doi.org/10.1080/07391102.2022.2158135


Binding studies of the water-soluble thiadicarbocyanine dye 3,3’-diethylthiadicarbocyanine acetate (DTC) with bovine serum albumin (BSA) were examined under physiological conditions using spectroscopic techniques like fluorescence, UV-Visible, circular dichroism (CD), FT-IR and molecular docking methods. Compiled experimental results envisage that DTC quench the fluorescence intensity of BSA. The increasing binding constants (K) were found to be in the order of 103 Mol−1 as a function of temperature, as calculated from the fluorescence quenching data. The quenching mechanism, thermodynamic parameters (ΔH0, ΔS0 and ΔG0) and the number of binding sites have been explored. CD values showed that the secondary structure of the BSA has been altered upon binding to DTC. Displacement experiments were carried out with different site probes to find out the binding site of DTC on BSA and it was found that binding interaction at site II of sub-domain IIIA. The interference of common metal ions on the interaction of DTC with BSA has also been studied. The experimental data exhibit that DTC interacts with BSA by hydrophobic forces. The experimental findings from BSA binding studies were validated by using in silico molecular docking technique. The results of the investigations were accurately supported by studies on molecular docking. The optimal shape of the molecular probe demonstrated the affinity as a free binding energy release of −7.37 Kcal/mol. The present research report endeavors to the approachable nature of water-soluble DTC dye and paves way for targeted biological interactions. Communicated by Ramaswamy H. Sarma.

Item Type: Journal Article
Publication: Journal of Biomolecular Structure and Dynamics
Publisher: Taylor and Francis Ltd.
Additional Information: The copyright for this article belongs to Taylor and Francis Ltd.
Keywords: binding interaction; bovine serum albumin; hydrophobic forces; Liquid crystal; molecular docking
Department/Centre: Division of Interdisciplinary Sciences > Computational and Data Sciences
Date Deposited: 29 Jan 2023 06:41
Last Modified: 29 Jan 2023 06:41
URI: https://eprints.iisc.ac.in/id/eprint/79571

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