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 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.
Stan
Dana
D
Department of Organic Chemistry, Bucharest University, Sos. Panduri, Romania. dana_stan2005@yahoo.com
Matei
Iulia
I
Mihailescu
Carmen
C
Savin
Mihaela
M
Hillebrand
Mihaela
M
Baciu
Ion
I
Matache
Mihaela
M
D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D004735:Energy Transfer; D006801:Humans; D007189:Indans / Q000737:chemistry*; D015394:Molecular Structure; D011485:Protein Binding; D011487:Protein Conformation; D012709:Serum Albumin / Q000737:chemistry*; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013050:Spectrometry, Fluorescence
C413384:1,2-indanedione; D007189:Indans; D012709:Serum Albumin; D012710:Serum Albumin, Bovine