Interactions of the carrier ligands of antidiabetic metal complexes with human serum albumin: A combined spectroscopic and separation approach with molecular modeling studies
- Author(s)
- Eva Anna Enyedy, Laszlo Horvath, Anasztazia Hetenyi, Tiziano Tuccinardi, Christian Hartinger, Bernhard Keppler, Tamas Kiss
- Abstract
The specific binding of carrier ligands of antidiabetic vanadium(IV) and zinc(II) complexes into drug binding pockets of human serum albumin (HSA) has been investigated via displacement reactions of site markers such as warfarin and dansylglycine by different spectroscopic (fluorescence, circular dichroism, NMR) and separation methods (capillary zone electrophoresis, ultrafiltration-UV). Conditional stability constants of the ligands were calculated for the binding at sites I and II of HSA. Binding site I was found to be the primary binding site for 2,6-pyridine dicarboxylic acid (dipic) and picolinic acid (pic), and site II for 6-methylpicolinic acid (6-Mepic) and maltol, although dipic, 6-Mepic and pic displace both site markers at differing extents. The experimental data is complemented by protein-ligand docking calculations for dipic and 6-Mepic which support the observations.
- Organisation(s)
- Department of Inorganic Chemistry
- External organisation(s)
- University of Szeged, University of Pisa
- Journal
- Bioorganic & Medicinal Chemistry
- Volume
- 19
- Pages
- 4202-4210
- No. of pages
- 9
- ISSN
- 0968-0896
- DOI
- https://doi.org/10.1016/j.bmc.2011.05.063
- Publication date
- 2011
- Peer reviewed
- Yes
- Austrian Fields of Science 2012
- 104003 Inorganic chemistry, 301303 Medical biochemistry
- Portal url
- https://ucrisportal.univie.ac.at/en/publications/eb2a0237-c96f-4dac-bb2b-5f0cce36de8d