Skip navigation
  • Logo
  • Home
  • Communities
    & Collections
  • Research Outputs
  • Researchers
  • Projects
  • Explore by
    • Research Outputs
    • Researchers
    • Projects
  • Sign on to:
    • My DSpace
    • Receive email
      updates
    • Edit Account details
FFH logo

  1. RePhyChem
  2. Research Outputs
  3. Journal Article
Please use this identifier to cite or link to this item: https://dspace.ffh.bg.ac.rs/handle/123456789/202
Title: Binding of doxyl stearic spin labels to human serum albumin: an EPR study
Authors: Pavićević, Aleksandra 
Popović Bijelić, Ana 
Mojović, Miloš 
Šušnjar, Snežana V
Bačić, Goran G
Issue Date: 18-Sep-2014
Journal: The journal of physical chemistry. B
Abstract: 
The binding of spin-labeled fatty acids (SLFAs) to the human serum albumin (HSA) examined by electron paramagnetic resonance (EPR) spectroscopy was studied to evaluate the potential of the HSA/SLFA/EPR technique as a biomarking tool for cancer. A comparative study was performed on two spin labels with nitroxide groups attached at opposite ends of the fatty acid (FA) chain, 5-doxyl stearic (5-DS) and 16-doxyl stearic (16-DS) acid. The effects of incubation time, different [SLFA]/[HSA] molar ratios, ethanol, and temperature showed that the position of the nitroxide group produces certain differences in binding between the two SLFAs. Spectra for different [SLFA]/[HSA] molar ratios were decomposed into two spectral components, which correspond to the weakly and strongly bound SLFAs. The reduction of SLFA with ascorbate showed the existence of a two component process, fast and slow, confirming the decomposition results. Warfarin has no effect on the binding of the two SLFAs, whereas ibuprofen significantly decreases the binding of 5-DS and has no effect on 16-DS. Together, the results of this study indicate that both SLFAs, 5-DS and 16-DS, should be used for the study of HSA conformational changes in blood induced by various medical conditions.
URI: https://dspace.ffh.bg.ac.rs/handle/123456789/202
ISSN: 1520-6106
DOI: 10.1021/jp5068928
Appears in Collections:Journal Article

Show full item record

SCOPUSTM   
Citations

21
checked on Jun 11, 2025

Page view(s)

22
checked on Jun 11, 2025

Google ScholarTM

Check

Altmetric

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.


Explore by
  • Communities
    & Collections
  • Research Outputs
  • Researchers
  • Projects
University of Belgrade
Faculty of Physical Chemistry
Studentski trg 12-16
11158 Belgrade 118
PAC 105305
SERBIA
University of Belgrade Faculty of Physical Chemistry