Alterations in the structure of blood carrier protein of Albumin upon interaction with new synthesized Pt(II) complex

In recent years, using heavy metal compounds such as platinum as anticancer agent is one of the commonways in cancer chemical therapy. In this study, the biological evaluation of a new anticancer compound ofglycine derivative of Pt(II) complex was investigated again Human serum albumin (HSA) as a mostabundant and carrier protein in plasma. The side effects of this novel compound was checked via itsability on the alterations in the function and structure of HSA at different temperatures of 25 and 37°C byapplying various spectroscopic (fluorescence, Far UV circular dichroism (CD) and UV visible) methods.Fluorescence data indicated the strong ability of Pt(II) complex to quench the intrinsic fluorescence ofHSA.The binding parameters and thermodynamic parameters, including ΔH°, ΔS°, and ΔG° were alsocalculated by the fluorescence quenching method.The Fluorescence results have shown that there is onebinding site on HSA forbinding of this complex. Also, thermal denaturation data of the protein in theabsecnce and presence of this complex represented the reduction of protein thermal stability uponinteraction with the Pt(II) complex via reducing of Tm value of protein. Our results suggest that the newsynthesized Pt(II) complex can bind to the blood carrier protein of HSA and change the stability andtertiarystructures of protein without any alterations in secondary structure, which can be considered as theside effects of this new synthesized drugs.

کلیدواژه ها:

Human serum albumin ، Pt(II) complex ، cancer ، fluorescence quenching