کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
5398824 1505893 2015 8 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Biophysical study on the interaction between two palladium(II) complexes and human serum albumin by Multispectroscopic methods
موضوعات مرتبط
مهندسی و علوم پایه شیمی شیمی تئوریک و عملی
پیش نمایش صفحه اول مقاله
Biophysical study on the interaction between two palladium(II) complexes and human serum albumin by Multispectroscopic methods
چکیده انگلیسی
The interaction of [Pd(bpy)(n-pr-dtc)]Br (I) and ([Pd(phen)(n-pr-dtc)]Br (II) (bpy=2,2′-bipyridine, phen=1,10-phenanthroline and n-pr-dtc=n-propyldithiocarbamate) with human serum albumin (HSA) was investigated using fluorescence, UV-vis absorption and circular dichroism (CD) spectroscopy techniques under simulative physiological conditions (pH=7.4). It was observed that the two complexes interact with HSA via static fluorescence quenching. The thermodynamic parameters indicate that the binding process was spontaneous and that hydrogen bonds and van der Waals forces play a major role in the association of the HSA-Pd(II) complexes. The activation energy (Ea), binding constant (Kb) and number of binding sites (n) of the HSA-Pd(II) complexes were calculated from fluorescence data at 293 K, 303 K and 311 K. The conformational alternations of protein secondary structure in the presence of Pd(II) complexes were demonstrated using synchronous fluorescence, three-dimensional fluorescence spectra, UV-vis absorption and circular dichroism techniques. Furthermore, the apparent distance between donor (HSA) and acceptor (Pd(II) complexes) was determined using fluorescence resonance energy transfer (FRET). The binding studies between these complexes and HSA give us key insights into the transportation, distribution and toxicity of newly design antitumor Pd(II) complexes in human blood.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Luminescence - Volume 167, November 2015, Pages 391-398
نویسندگان
, , ,