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Spectroscopic, zeta potential and molecular docking analysis on the interaction between human serum albumin and halogenated thienyl chalcones

Publication Type : Journal Article

Publisher : Journal of Molecular Liquids

Source : Journal of Molecular Liquids, Volume 242, p.1018-1026 (2017)

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Keywords : human serum albumin, molecular docking, Spectroscopy, Thiophene chalcone, zeta potential

Campus : Kochi

School : School of Pharmacy

Center : Amrita Institute of Medical Science

Department : Pharmaceutical Chemistry & Analysis, Pharmacology, Pharmacy Practice

Year : 2017

Abstract : The interaction between halogenated thiophene chalcones and the main plasma protein, i.e. human serum albumin (HSA), has been investigated in vitro under simulated physiological condition by spectroscopic techniques (UV–Vis, fluorescence and circular dichroism), zeta potential and molecular docking. Fluorescence quenching of albumin by the thiophene chalcones T1–T9 (kq≈1012M−1s−1) indicates a static quenching mechanism; however, for the samples T02 and T5 the possibility of a combination of simultaneous static and dynamic quenching mechanism was detected. According to FRET theory, the energy transfer from HSA to the thiophene chalcones occurs with high probability. Modified Stern-Volmer binding constants (Ka≈104M−1), circular dichroism and potential surface data suggest that the association HSA:thiophene chalcone is moderate and there is not a significant perturbation on the secondary structure of albumin, as well as on its surface. Thermodynamic parameters indicate a spontaneous (ΔG°<0) and a probably entropy-driven (ΔS°<0) association, typical of hydrophobic interactions. On the other hand, for T5 besides the entropy-driven association there is also a contribution from the enthalpy change (ΔH°<0). Molecular docking results suggest hydrogen bonding and hydrophobic interactions as the main binding forces in the association between HSA and all thiophene chalcones; however, molecular docking calculations for T05 detected a high possibility of an electrostatic interaction between the fluorine atom and the Lys-194 residue.

Cite this Research Publication : O. Augusto Chaves, Bijo Mathew, Cesarin-Sobrinho, D., Lakshminarayanan, B., Joy, M., Mathew, G. Elizabeth, Suresh, J., and Netto-Ferreira, J. Carlos, “Spectroscopic, zeta potential and molecular docking analysis on the interaction between human serum albumin and halogenated thienyl chalcones”, Journal of Molecular Liquids, vol. 242, pp. 1018-1026, 2017.

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