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Spectroscopic Investigation on the Binding of the Antitumoral Pd(II) Complex to Human Serum Albumin
Author(s) -
Saeidifar Maryam,
MansouriTorshizi Hassan,
Divsalar Adeleh,
Saboury Ali.Akbar
Publication year - 2013
Publication title -
journal of the chinese chemical society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.329
H-Index - 45
eISSN - 2192-6549
pISSN - 0009-4536
DOI - 10.1002/jccs.201200122
Subject(s) - chemistry , circular dichroism , quenching (fluorescence) , human serum albumin , fluorescence , binding constant , complex formation , absorption (acoustics) , crystallography , stereochemistry , binding site , biochemistry , inorganic chemistry , physics , quantum mechanics , acoustics
The interaction of human serum albumin (HSA) with 1,10‐phenanthroline‐ethyldithiocarbamatopalladium(II) nitrate complex, [Pd(phen)(Et‐dtc)]NO 3 , has been studied by using absorption, fluorescence and circular dichroism spectroscopic measurements. UV‐Vis studies imply that The peptide strands of protein molecules extended more (denatured) upon the addition of Pd(II) complex. This process is spontaneous and exothermic. A fluorescence quenching reaction of Pd(II) complex and HSA was observed and quenching mechanism was suggested as static quenching according to Stern‐Volmer equation. The number of binding sites (n) and apparent association constant (K A ) were calculated using fluorescence quenching data. The circular dichroism results revealed the conformational changes in secondary structure of protein upon its interaction with Pd(II) complex. In these interaction studies, several thermodynamic and binding parameters are also determined which may provide deeper insights into structural changes induced by an antitumor Pd(II) complex on the protein as the metal complex side effects.