Bovine serum albumin interactions with metal complexes

Authors

  • Tamara Topală
  • Andreea Bodoki
  • Luminiţa Oprean
  • Radu Oprean

DOI:

https://doi.org/10.15386/cjmed-357

Keywords:

drug-protein interaction, coordination complex, fluorescence spectroscopy, UV-Vis absorption spectroscopy

Abstract

The continuous search for new molecules with therapeutic abilities has led to the synthesis and characterization of a large number of metal complexes, proven to exhibit potential as pharmacological agents through their antibacterial, antiviral, antifungal and antineoplastic properties. As serum albumins play a key role in drug pharmacokinetics and pharmacodynamics, the study of coordination compounds affinity towards this class of proteins, as well as understanding the mechanism through which they interact is crucial. The aim of this review is to focus on the structure and biological functions of bovine serum albumin, the design of metal complexes that are able to bind to the biomolecule, as well as the experimental techniques employed in the study and evaluation of these interactions. Keywords: drug-protein interaction, coordination complex, fluorescence spectroscopy, UV-Vis absorption spectroscopy.

Author Biographies

Tamara Topală, "Iuliu Haţieganu" University of Medicine and Pharmacy Cluj-Napoca

Department of General and Inorganic Chemistry

Andreea Bodoki, "Iuliu Haţieganu" University of Medicine and Pharmacy Cluj-Napoca

Department of General and Inorganic Chemistry

Luminiţa Oprean, "Iuliu Haţieganu" University of Medicine and Pharmacy Cluj-Napoca

Department of General and Inorganic Chemistry

Radu Oprean, "Iuliu Haţieganu" University of Medicine and Pharmacy Cluj-Napoca

Department of Analytical Chemistry and Instrumental Analysis

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Published

2014-11-12

How to Cite

1.
Topală T, Bodoki A, Oprean L, Oprean R. Bovine serum albumin interactions with metal complexes. Med Pharm Rep [Internet]. 2014 Nov. 12 [cited 2025 Oct. 6];87(4):215-9. Available from: https://medpharmareports.com/index.php/mpr/article/view/357

Issue

Section

Reviews