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Spectroscopic Investıgations On Dna And Bsa Binding Ability Of A New Platinum (Iı) Complex Containing 5,6-Dı(Pyridin-2-Yl)-2,3-Dihydropyrazine Ligand

BROWSE_DETAIL_CREATION_DATE: 09-08-2017

BROWSE_DETAIL_IDENTIFIER_SECTION

BROWSE_DETAIL_TYPE: Thesis

BROWSE_DETAIL_SUB_TYPE: Masters

BROWSE_DETAIL_PUBLISH_STATE: Unpublished

BROWSE_DETAIL_FORMAT: PDF Document

BROWSE_DETAIL_LANG: English

BROWSE_DETAIL_SUBJECTS: Chemical technology, Chemical engineering,

BROWSE_DETAIL_CREATORS: Salem, Asma Mabrouk Mohamed (Author),

BROWSE_DETAIL_CONTRIBUTERS: Özalp Yaman, Şeniz (Advisor),

BROWSE_DETAIL_TAB_KEYWORDS

Antitumor drugs, platinum complexes, -nitrogen donor ligands, DNA binding ability, BSA binding ability


BROWSE_DETAIL_TAB_ABSTRACT

Designing and synthesis of more effective and less toxic platinum complexes are one of the main aims of the researchers to overcome the side effects of the cisplatinum chemotherapy. For this purpose, a new platinum(II) complex containing 2,3-bis(2-pyridyl)-5,6-dihydropyrazine (PtLCl2) was modelled to mimic the cisplatinum structure , then synthesized and identified by several spectroscopic techniques to assess its DNA and BSA binding ability in this work.In order to elucidate the type of association of the complex to calf thymus DNA, UV titration, fluorometric titration, thermal decomposition and viscometry experiments were conducted under physiological conditions. Thermodynamic parameters were also determined from the UV titrations which are iterated at different temperatures. It is found that PtLCl2 interacts with DNA through groove binding or electrostatically.Binding ability of PtLCl2 to BSA (Bovine Serum Albumin) was also tested with the similar techniques that were used formerly in the DNA association studies. The results clearly indicated that the complex interacted with the hydrophobic region of the protein electrostatically leading an increase in hydrophilicity of the protein.ivThe IR analysis made specifically for identifying the binding side of the complex to BSA were also confirmed increasing in the hydrophilicity of the protein with the effect of PtLCl2.


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