Investigation of interaction between [Pd(en)(2-pyc)]NO3 and bovine serum albumin (BSA) using fluorescence spectroscopy

سال انتشار: 1397
نوع سند: مقاله کنفرانسی
زبان: انگلیسی
مشاهده: 336

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شناسه ملی سند علمی:

IICC20_095

تاریخ نمایه سازی: 2 تیر 1398

چکیده مقاله:

Many drugs are transported in the blood while bound to albumin. Therefore, investigation of the Drug-protein interaction is important to know mechanism of the transport of a drug in the body. In the present study, bovine serum albumin (BSA) has been used as the protein model because of the abundance, cheapness and similarity with the human serum albumin[1]. Herein, the interaction between a recently made palladium(II) complex of formula [Pd(en)(2-pyc)]NO3 (where en = 1,2-diaminoethane and 2-pyc = 2-pyridinecarboxylate anion), as a potential anti-tumor agent, and BSA was studied by fluorescence spectroscopy. The fluorescence titration experiments in Tris-HCl buffer of pH = 7.00 were performed at a fixed BSA concentration while varying the concentration of metal complex. The obtained data indicated that the Pd(II) complex strongly quench the intrinsic fluorescence of BSA. Analyzing of the data using Stern–Volmer equation, the quenching constant (Ksv), binding constant (Kb), number of binding sites (n) and the bimolecular quenching rate constant (kq) have been calculated. Using these date, thermodynamic parameters were calculated too. Decreasing the equilibrium rate constants with increasing the temperature indicates that the quenching mechanism of BSA by the Pd(II) complex is static quenching. The negative values of ΔHº and ΔSº show that hydrogen bonds and van der Waals force play a major role in the binding of the Pd(II) complex to BSA [2].

نویسندگان

Nasimeh Jamgohari,

Department of Chemistry, University of Sistan and Baluchestan, Zahedan, Iran

Khatereh Abdi

Department of Chemistry, University of Sistan and Baluchestan, Zahedan, Iran