Maghemite nanoparticles coated with human serum albumin: combining targeting by the iron-acquisition pathway and potential in photothermal therapies

2017 ◽  
Vol 5 (17) ◽  
pp. 3154-3162 ◽  
Author(s):  
J. Hai ◽  
H. Piraux ◽  
E. Mazarío ◽  
J. Volatron ◽  
N. T. Ha-Duong ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Ligand Binding ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Iron Acquisition ◽  
Maghemite Nanoparticles ◽  
Ligand Binding Sites ◽  
Transport Vehicle ◽  
Multiple Ligand

Human serum albumin (HSA), the most abundant plasma protein in human blood, is a natural transport vehicle with multiple ligand binding sites.

scholarly journals Differential Effects of Methoxy Group on the Interaction of Curcuminoids with Two Major Ligand Binding Sites of Human Serum Albumin

PLoS ONE ◽  
2014 ◽  
Vol 9 (2) ◽  
pp. e87919 ◽  
Author(s):  
Hiroki Sato ◽  
Victor Tuan Giam Chuang ◽  
Keishi Yamasaki ◽  
Noriyuki Yamaotsu ◽  
Hiroshi Watanabe ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Ligand Binding ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Methoxy Group ◽  
Differential Effects ◽  
Ligand Binding Sites

scholarly journals Ligand-binding properties of proalbumin Christchurch

1980 ◽  
Vol 191 (1) ◽  
pp. 281-283 ◽  
Author(s):  
R G Reed ◽  
T Peters ◽  
S O Brennan ◽  
R W Carrell
Keyword(s):  
Fatty Acids ◽  
Human Serum Albumin ◽  
Ligand Binding ◽  
Serum Albumin ◽  
Human Serum ◽  
Protein Conformation ◽  
Binding Sites ◽  
Bromocresol Green ◽  
Binding Properties ◽  
Normal Albumin

Proalbumin Christchurch, a circulating variant of human serum albumin, is secreted from the liver without cleavage of the hexapeptide situated at the N-terminal end of the peptide chain of proalbumin. We compared ligand-binding properties of proalbumin Christchurch and of normal albumin A from the same individual in order to test the effect of the presence of the hexapeptide. The two albumin forms exhibited similar affinities for palmitate, bilirubin, 8-anilinonaphthalene-1-sulphonate and Bromocresol Green. The patterns of endogenous fatty acids bound to the two forms of albumin were slightly different, although the differences were probably not of physiological significance. From these studies it would appear that the propeptide of proalbumin does not alter the protein conformation in such a way as to alter binding sites for organic anions.

scholarly journals Comparative studies of the binding of some ligands to human serum albumin non-covalently attached to immobilized Cibacron Blue, or covalently immobilized on Sepharose, by column affinity chromatography

1983 ◽  
Vol 213 (2) ◽  
pp. 387-390 ◽  
Author(s):  
C Lagercrantz ◽  
T Larsson
Keyword(s):  
Fatty Acids ◽  
Salicylic Acid ◽  
Human Serum Albumin ◽  
Complex Formation ◽  
Ligand Binding ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Binding Strength ◽  
Cibacron Blue

A comparative study of the ligand-binding properties of human serum albumin was performed by the technique of affinity chromatography with the protein attached to immobilized Cibacron Blue F3GA (Blue Sepharose), or covalently immobilized on Sepharose. The binding strength of octanoate, decanoate and dodecanoate is much weaker when human serum albumin is attached to immobilized Cibacron Blue, indicating that the binding sites for fatty acids are involved in the attachment of human serum albumin to immobilized Cibacron Blue. The results revealed additional alterations of the ligand binding when human serum albumin was attached to immobilized Cibacron Blue, involving sites outside of the binding domains of fatty acids. Thus the stereoselective binding of L-tryptophan was abolished, and the resolution of the warfarin enantiomers was impaired. However, the binding strength of warfarin and salicylic acid was rather close to the values observed with human serum albumin covalently immobilized on Sepharose. It is suggested that the availability of the binding sites for L-tryptophan, warfarin and salicylic acid is partially blocked by the complex between albumin and the dye without direct participation in the complex-formation. An alternative interpretation involves an allosteric mechanism brought about by complex-formation between serum albumin and the immobilized Cibacron Blue.

Zinc–human serum albumin association: testimony of two binding sites

Talanta ◽  
2004 ◽  
Vol 63 (2) ◽  
pp. 503-508 ◽  
Author(s):  
C. André ◽  
Y.C. Guillaume
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites

scholarly journals Characterization of the binding sites of the anticancer ruthenium(III) complexes KP1019 and KP1339 on human serum albumin via competition studies

2012 ◽  
Vol 18 (1) ◽  
pp. 9-17 ◽  
Author(s):  
Orsolya Dömötör ◽  
Christian G. Hartinger ◽  
Anna K. Bytzek ◽  
Tamás Kiss ◽  
Bernhard K. Keppler ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites

scholarly journals Identifying Steroid Hormone Binding Sites on Human Serum Albumin by 2D NMR

2013 ◽  
Vol 104 (2) ◽  
pp. 430a ◽  
Author(s):  
Eileen S. Krenzel ◽  
Heidi A. Schwanz ◽  
Ravi Jasu ◽  
Michael Zakharov ◽  
Shalendar Bhasin ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Steroid Hormone ◽  
2D Nmr ◽  
Hormone Binding
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