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Influence of the oxidation state of the metal center on the interaction of ruthenium complex with HSA

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Abstract

The binding of [Ru(H2O)2(bpydip)]2+/3+ (bpydip = N,N′-bis[1-(2-pyridinyl)ethylidene]-1,3-propanediamine) to human serum albumin was investigated by spectroscopic techniques. The hydrophobic interaction between ruthenium(II) complex and HSA was spontaneous with the binding constants calculated to be 1.27 × 103 dm3 mol−1 (298 K), 7.74 × 103 dm3 mol−1 (303 K), and 9.46 × 103 dm3 mol−1 (308 K). The binding of ruthenium(III) complex to HSA induced the hybrid quenching mechanism with the binding constants estimated to be 1.25 × 109 dm3 mol−1 (298 K), 1.31 × 109 dm3 mol−1 (303 K), and 3.57 × 109 dm3 mol−1 (308 K). Thermodynamic parameters (ΔH = 76 kJ mol−1; ΔS = 515 J mol−1 K−1) indicated that hydrophobic forces played a major role in the binding of ruthenium(III) complex to HSA. In addition, the number of binding sites (n) for ruthenium(II) complex was approximately 1, whereas ruthenium(III) complex recorded 2. CD data indicated that the secondary structure of HSA is not changed in the presence of complexes.

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Acknowledgments

We are grateful to CNPq for financial support.

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Authors and Affiliations

  1. Departamento de Química, Universidade Estadual de Maringá, Maringa, Brazil

    Douglas Santana Franciscato & Vagner Roberto de Souza

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  1. Douglas Santana Franciscato
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  2. Vagner Roberto de Souza
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Correspondence to Vagner Roberto de Souza.

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Franciscato, D.S., de Souza, V.R. Influence of the oxidation state of the metal center on the interaction of ruthenium complex with HSA. Monatsh Chem 147, 1315–1321 (2016). https://doi.org/10.1007/s00706-016-1659-0

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