title

مطالعه اندرکنش ماده ضد سرطان جدید کمپلکس (Pd II) با دمهای آلیفاتیک آلبومین سرم انسانی

دیوسالار, عادله and باقری, محمد جواد and صبوری, علی اکبر and منصوری ترشیزی, حسن and امانی, مجتبی (1388) مطالعه اندرکنش ماده ضد سرطان جدید کمپلکس (Pd II) با دمهای آلیفاتیک آلبومین سرم انسانی. J. Phys. Chem. B ــ 113 (42). pp. 14035-14042. شاپا 1520-6106

[img] Text - Published Version
محدود به Repository staff only

837kB
[img]
Preview
Text - Published Version
57kB

Official URL: http://pubs.acs.org/toc/jpcbfk/113/42


Title

Investigation on the Interaction of Newly Designed Anticancer Pd(II) Complexes with Different Aliphatic Tails and Human Serum Albumin

English Abstract

The pharmacokinetics and pharmacodynamics of any drug will depend, largely, on the interaction that it has with human serum albumin (HSA), the most abundant plasma protein. The interaction between newly synthesized Pd(II) complexes, 2,2′-bipyridin octyl dithiocarbamato Pd(II) nitrate (Octpd), 2,2′-bipyridin butyl dithiocarbamato Pd(II) nitrate (ButPd), 2,2′-bipyridin ethyl dithiocarbamato Pd(II) nitrate (EtPd), antitumor components, with human serum albumin, a carrier protein, were studied at different temperatures of 27 and 37 °C by fluorescence spectroscopy, far UV circular dichroism (CD), and spectrophotometric and differential scanning calorimetry (DSC) techniques. By the analysis of fluorescence intensity, it was observed that Pd(II) complexes have strong abilities to quench the intrinsic fluorescence of HSA through a dynamic quenching procedure. The binding parameters were evaluated by the fluorescence quenching method. The thermodynamic parameters, including ΔH°, ΔS°, and ΔG°, were calculated by the fluorescence quenching method and indicated that hydrophobic forces play a major role in the interaction of Pd(II) complexes with HSA. Far-UV-CD results represented that Pd(II) complexes induced a decrease in content of the R helical structure of protein. The binding of newly designed drugs (Pd(II) complexes) on the blood carrier protein of HSA resulted in significant alterations on the structure and conformation of protein via decreasing stability of HSA by decreasing the Tm, a red shift in maximum fluorescence intensity, a decrease in content of the R-helical structure, and the increase of the nonpolar or accessible hydrophobic surface of HSA to solvent.

Item Type:Article
زبان سند : انگلیسی
نویسنده مسئول :عادله دیوسالار
Additional Information: 2008 Impact Factor: 4.189 Indexed/Abstracted in: 1- Medline/PubMed - ISI- 2- SCOPUS, 3-CAS, EBSCOhos, Proquest, British Library, , Ovid, SwetsWise.
Subjects:QV pharmacology
QU Biochemistry
Divisions:Faculty of Medicine > Department of Basic Sciences > Department of Biophysics
ID Code:1060
Deposited By: MS Soghra Golmaghani
Deposited On:13 Dec 1388 05:19
Last Modified:20 Jan 1393 12:48

Repository Staff Only: item control page

Document Downloads

More statistics for this item...