4.4 Article

Interactions of a Ruthenium-Ketoprofen Compound with Human Serum Albumin and DNA: Insights from Spectrophotometric Titrations and Molecular Docking Calculations

Journal

CHEMISTRYSELECT
Volume 7, Issue 4, Pages -

Publisher

WILEY-V C H VERLAG GMBH
DOI: 10.1002/slct.202104020

Keywords

albumin; DNA; ketoprofen; molecular docking; ruthenium

Funding

  1. Fundacao de Amparo a Pesquisa do Estado de Sao Paulo, FAPESP [2018/18060-3, 2019/04173-3]
  2. Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior, CAPES [001]
  3. Conselho Nacional de Desenvolvimento Cientifico e Tecnologico, CNPq [306004/2018-6]
  4. Fundacao para a Ciencia e a Tecnologia (FCT - Portuguese Foundation for Science and Technology) [2020.07504.BD]
  5. Fundação para a Ciência e a Tecnologia [2020.07504.BD] Funding Source: FCT

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This study found that the compound [Ru2O(keto)(2)(py)(6)](PF6)(2) interacts with both DNA and HSA, with a stronger interaction with HSA. The interaction occurs mainly through a static mechanism and is enthalpically driven. The molecular docking results also support these observations.
The compound [Ru2O(keto)(2)(py)(6)](PF6)(2), keto=ketoprofen and py=pyridine, interacts with calf thymus-DNA with K-b=1.08x10(4) M-1. It efficiently quenches HSA fluorescence in different temperatures, with Ksv values in the 10(4)-10(5) M-1 range, both by dynamic and static mechanisms. The data provided by the double logarithmic and van't Hoff approximations indicated a moderate (K-b approximate to 10(4) M-1) and spontaneous (Delta G<0) interaction, being enthalpically driven (Delta H=-27.1 kJ mol(-1) and Delta S=-5.3 J mol(-1) K-1). Molecular docking calculations confirmed that the binuclear compound interacts with HSA more strongly than with DNA. The occurrence of a high contribution from electrostatic forces was observed, fully consistent with the bicationic nature of [Ru2O(keto)(2)(py)(6)](PF6)(2). The molecular docking results also revealed that the interaction occurs in an external subdomain, explaining the lack of significant conformational changes in the protein, as probed by circular dichroism spectra.

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