Journal
JOURNAL OF MOLECULAR LIQUIDS
Volume 242, Issue -, Pages 1018-1026Publisher
ELSEVIER
DOI: 10.1016/j.molliq.2017.07.091
Keywords
Thiophene chalcone; Human serum albumin; Spectroscopy; Zeta potential; Molecular docking
Funding
- CAPES (Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior)
- CNPq (Conselho Nacional de Desenvolvimento Cientifico e Tecnologico) [485631-2012]
- FAPERJ (Fundacao de Amparo Pesquisa do Estado do Rio de Janeiro) [E-26/11.570]
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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 (k(q) approximate to 10(12) M(-1)s(-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 (K-a approximate to 10(4) M-1), circular dichroism and poteritial 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 (Delta G degrees < 0) and a probably entropy-driven (Delta S degrees < 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 (Delta H degrees < 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. (C) 2017 Elsevier B.V. All rights reserved.
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