Investigation of the Binding Behavior between the S-heterocyclic Aromatic Palladium(II) Complex and Human Serum Albumin: Spectroscopic Approach |
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| Authors: | Maryam Saeidifar A Khanlarkhani M Eslami-Moghaddam Hassan Mansouri-Torshizi Ali Akbar Saboury |
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| Affiliation: | 1. Department of Nanotechnology and Advanced Materials, Materials and Energy Research Center, Karaj, Iran;2. Chemistry and Chemical Engineering Research Center, Tehran, Iran;3. Department of Chemistry, University of Sistan and Baluchestan, Zahedan, Iran;4. Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran |
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| Abstract: | The interaction of 1, 10-phenanthroline octhyldithiocarbamato palladium(II) nitrate (Pd(Oct-dtc)(phen)]NO3) with human serum albumin (HSA) has been investigated by various spectroscopic techniques under physiological conditions. Here, HSA was titrated with the Pd(II) complex, followed by UV–Vis absorption spectroscopy to estimate a binding constant (Kb) and other thermodynamic parameters. The results indicate that the Pd (II) complex has a high affinity for bind HSA. Thermodynamic analysis showed that the enthalpy (ΔH°) and entropy changes (ΔS°) are positive and Gibbs free energy change (ΔG°) is negative which indicated that hydrophobic interactions played the predominant role in the binding process. Fluorescence spectroscopy were used to show the mechanism and binding parameters of this interaction. Utilizing the Stern–Volmer equation, the Pd(II) complex quenched the intrinsic fluorescence of HSA via a static quenching procedure. The specific binding distances between the tryptophan (donor) proteins and Pd(II) complex (acceptor) were estimated by Forster resonance energy transfer. The CD results also showed the conformational changes on serum albumin upon binding with the Pd(II) complex. |
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| Keywords: | energy transfer fluorescence human serum albumin palladium(ii) complex thermodynamic parameters |
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