Spectroscopic investigations of the binding interaction of a new indanedione derivative with human and bovine serum albumins

Binding of a newly synthesized indanedione derivative, 2-(2-hydroxy-3-ethoxybenzylidene)-1,3-indanedione (HEBID), to human and bovine serum albumins (HSA and BSA), under simulated physiological conditions was monitored by fluorescence spectroscopy. The binding parameters (binding constants and numbe...

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Published in:Molecules (Basel, Switzerland) Switzerland), 2009-04, Vol.14 (4), p.1614-1626
Main Authors: Stan, Dana, Matei, Iulia, Mihailescu, Carmen, Savin, Mihaela, Hillebrand, Mihaela, Baciu, Ion, Matache, Mihaela
Format: Article
Language:English
Subjects:
Animals
Anticoagulants
Binding sites
Biological activity
Cattle
Chemistry
Circular Dichroism
Energy Transfer
Fluorescence
Fluorescence resonance energy transfer
Humans
Indanedione
Indans - chemistry
Ligands
Molecular Structure
Pharmacokinetics
Physiology
Protein Binding
Protein Conformation
Proteins
Serum albumin
Serum Albumin - chemistry
Serum Albumin, Bovine - chemistry
Spectrometry, Fluorescence
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Summary:Binding of a newly synthesized indanedione derivative, 2-(2-hydroxy-3-ethoxybenzylidene)-1,3-indanedione (HEBID), to human and bovine serum albumins (HSA and BSA), under simulated physiological conditions was monitored by fluorescence spectroscopy. The binding parameters (binding constants and number of binding sites) and quenching constants were determined according to literature models. The quenching mechanism was assigned to a Förster non-radiative energy transfer due to the HEBID-SA complex formation. A slightly increased affinity of HEBID for HSA was found, while the number of binding sites is approximately one for both albumins. The molecular distance between donor (albumin) and acceptor (HEBID) and the energy transfer efficiency were estimated, in the view of Förster's theory. The effect of HEBID on the protein conformation was investigated using circular dichroism and synchronous fluorescence spectroscopies. The results revealed partial unfolding in the albumins upon interaction, as well as changes in the local polarity around the tryptophan residues.
ISSN:1420-3049
1420-3049
DOI:10.3390/molecules14041614