Effect of long-chain free fatty acids on the conformation of the human serum albumin-warfarin binding site as studied by circular dichroism

1984 ◽  
Vol 6 (4) ◽  
pp. 175-178 ◽  
Author(s):  
Bernard Sebille ◽  
Nicole Thuaud ◽  
Jean-Paul Tillement ◽  
Josée Brienne
Keyword(s):  
Fatty Acids ◽  
Circular Dichroism ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Free Fatty Acids ◽  
Human Serum ◽  
Binding Site ◽  
Circular Dichroïsm ◽  
Long Chain

Circular dichroism and fluorescence spectroscopic study on the interaction of bisdemethoxycurcumin and diacetylbisdemethoxycurcumin with human serum albumin

2010 ◽  
Vol 88 (2) ◽  
pp. 155-163 ◽  
Author(s):  
Fakhrossadat Mohammadi ◽  
Abdol-Khalegh Bordbar ◽  
Khosro Mohammadi ◽  
Adeleh Divsalar ◽  
Ali Akbar Saboury
Keyword(s):  
Circular Dichroism ◽  
Secondary Structure ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Site ◽  
Binding Parameters ◽  
Oh Groups ◽  
Fluorescence Measurements ◽  
Circular Dichroïsm

The interactions of bisdemethoxycurcumin (BDMC) as a bioactive constituent of turmeric and diacetylbisdemethoxycurcumin (DABC) as a novel synthetic derivative of curcumin with human serum albumin (HSA) have been investigated by fluorescence and circular dichroism (CD) spectroscopy. The binding parameters, including the number of substantive binding sites and the binding constants, have been estimated from the analysis of fluorescence measurements. The estimated binding parameters indicated that BDMC has higher affinity than DABC to bind HSA, suggesting the essential role of the phenolic OH groups of BDMC, which are acetylated in DABC. It was found that the binding site for BDMC and DABC is located in the vicinity of Trp-214 in subdomain IIA, which is the same as binding site for curcumin (CUR). The minor changes on the far-UV circular dichroism spectra resulted in partial changes in the calculated secondary structure contents of HSA. The negligible alteration in the secondary structure of HSA indicated that ligand-induced conformational changes are localized in the binding site and do not involve considerable changes in the protein folding. The visible CD spectra indicated that the optical activity observed during the ligand binding is due to induced-protein chirality.

The fluorescence and circular dichroism of proteins in reverse micelles: application to the photophysics of human serum albumin and N-acetyl-l-tryptophanamide

1996 ◽  
Vol 60 (3) ◽  
pp. 63-77 ◽  
Author(s):  
Daniel M. Davis ◽  
David McLoskey ◽  
David J.S. Birch ◽  
Paul R. Gellert ◽  
Rodney S. Kittlety ◽  
...  
Keyword(s):  
Circular Dichroism ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Reverse Micelles ◽  
Circular Dichroïsm
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