Bu kaydın yasal hükümlere uygun olmadığını düşünüyorsanız lütfen sayfa sonundaki Hata Bildir bağlantısını takip ederek bildirimde bulununuz. Kayıtlar ilgili üniversite yöneticileri tarafından eklenmektedir. Nadiren de olsa kayıtlarla ilgili hatalar oluşabilmektedir. MİTOS internet üzerindeki herhangi bir ödev sitesi değildir!

Synthesis, Characterization and Bınding Behaviour of Platinum(Iı) Complex Containing N-(Pyridine-2-Yl) Methylene Benzamine With Dna, Hsa and Bsa Using Spectroscopic Techniques

BROWSE_DETAIL_CREATION_DATE: 24-08-2017

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BROWSE_DETAIL_PUBLISH_STATE: Unpublished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: Chemistry,

BROWSE_DETAIL_CREATORS: Abdalla, Rema A İbrahim (Author),

BROWSE_DETAIL_CONTRIBUTERS: Özalp, Şeniz (Advisor),

BROWSE_DETAIL_TAB_KEYWORDS

Antitumor drugs, platinum complexes, DNA binding, BSA binding, HSA binding, FTIR analysis.


BROWSE_DETAIL_TAB_ABSTRACT

Because, the structural equivalences of cisplatin, (Pt(NH3)2Cl2, react with DNA in a similar manner with the parent drug, the new platinum based antitumor drug candidates are expected to show high antitumor activity that overcome the drug resistance and serious side effects. For this purpose, the PtCl2 complex of N-(pyridin-2-yl)methylene benzenamin ligand (L), was synthesized and characterized. The binding ability of the Pt(L)Cl2 to the calf thymus DNA and the serum albumins (BSA and HSA) were examined. In order to elucidate the mechanism of the action between the Pt(L)Cl2 complex and DNA, spectroscopic measurements were performed. The electronic absorption spectra, thermal behavior, viscosity and fluorometric titration of the Pt complex treated DNA indicated that the compound electrostatically associated with DNA. The spectroscopic and viscometric measurements also revealed that Pt(L)Cl2 interacts electrostatically with serum proteins too. The interaction is through the hydrophobic region of both proteins, where the polarity around a tryptophan residue increases and hydrophobicity of -helices increases accordingly. However no clear evidences were obtained from the detailed FTIR analysis to locate the interaction site of Pt(L)Cl2 on the protein.


BROWSE_DETAIL_TAB_TOC



BROWSE_DETAIL_TAB_DESCRIPTION



BROWSE_DETAIL_TAB_RIGHTS



BROWSE_DETAIL_TAB_NOTES



BROWSE_DETAIL_TAB_REFERENCES


BROWSE_DETAIL_TAB_REFERENCED_BYS

BROWSE_DETAIL_GOTO_LIST

 

TEXT_STATS

  • TEXT_RECORD_STATS
    • TEXT_STATS_THIS_MONTH: 0
    • TEXT_STATS_TOTAL: 2414
  • TEXT_ONLINE_STATS
    • TEXT_ONLINE_STATS_TOTALONLINEVISITOR: 38
    • TEXT_ONLINE_STATS_TOTALONLINEUSER: 0
    • TEXT_STATS_TOTAL: 38

LINK_STATS