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Merck

Bovine Serum Albumin Interactions with Metal Complexes.

Clujul medical (1957) (2014-01-01)
Tamara Topală, Andreea Bodoki, Luminiţa Oprean, Radu Oprean
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.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Albumin, Bovine Serum, Cohn Fraction, 30% Aqueous Solution
Sigma-Aldrich
Albumin, Bovine Serum, Fraction V, RIA and ELISA Grade
Sigma-Aldrich
Albumin, Bovine Serum, 30% Aqueous Solution, Stabilizer-Free
Sigma-Aldrich
Albumin, Bovine Serum, 30% Sterile-Filtered Aqueous Solution, Preservative-Free
Sigma-Aldrich
Bovine Serum Albumin, For use as a marker in SDS-PAGE
Sigma-Aldrich
Bovine Serum Albumin, lyophilized powder, ≥96% (agarose gel electrophoresis)
Sigma-Aldrich
Bovine Serum Albumin, lyophilized powder, ≥98% (agarose gel electrophoresis)
Sigma-Aldrich
Albumin, Bovine Serum, Fraction V, Fatty Acid-Poor, Endotoxin-Free
Sigma-Aldrich
Albumin, Bovine Serum, Fraction V, Fatty Acid-Free
Sigma-Aldrich
Albumin fraction V, (from bovine serum) for biochemistry
Sigma-Aldrich
Albumin, Bovine Serum, Fraction V, Modified Cohn, pH 5.2
Sigma-Aldrich
Bovine Serum Albumin, OmniPur® Grade, >= 99%, Fraction V, Cold Alcohol Isolation