Spectroscopic Investigations of the Binding Interaction of a New Indanedione Derivative with Human and Bovine Serum Albumins

Molecules

Dana Stan¹  Iulia Matei²  Carmen Mihailescu¹  Mihaela Savin³  Mihaela Matache¹  Mihaela Hillebrand² 

[1] Department of Organic Chemistry, Bucharest University, 00133, Sos. Panduri No. 90-92, Romania; E-mails:;Department of Physical Chemistry, Faculty of Chemistry, University of Bucharest, Bd. Regina Elisabeta, No. 4-12, Bucharest, Romania; E-mails:;Telemedica, Str. Ion Calin, No.13, Bucharest, Romania; E-mail:

关键词: Indanedione;    Serum albumin;    Fluorescence;    Circular dichroism;    Fluorescence resonance energy transfer;   

DOI  :  10.3390/molecules14041614

来源: mdpi

【 摘 要 】

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.

【 授权许可】

CC BY   
© 2009 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland.