Toxic effects of chrysoidine on human serum albumin: isothermal titration calorimetry and spectroscopic investigations

Luminescence ◽  
2015 ◽  
Vol 31 (2) ◽  
pp. 335-340 ◽  
Author(s):  
Haoyu Sun ◽  
Yingxue Liu ◽  
Meng Li ◽  
Songlin Han ◽  
Xudan Yang ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Isothermal Titration Calorimetry ◽  
Toxic Effects ◽  
Titration Calorimetry ◽  
Spectroscopic Investigations

scholarly journals Multi-site binding of epigallocatechin gallate to human serum albumin measured by NMR and isothermal titration calorimetry

2017 ◽  
Vol 37 (3) ◽  
Author(s):  
Joshua D. Eaton ◽  
Mike P. Williamson
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Isothermal Titration Calorimetry ◽  
Epigallocatechin Gallate ◽  
Titration Calorimetry ◽  
Physiological Conditions ◽  
Almost All ◽  
Site Binding

The affinity of epigallocatechin gallate (EGCG) for human serum albumin (HSA) was measured in physiological conditions using NMR and isothermal titration calorimetry (ITC). NMR estimated the Ka (self-dissociation constant) of EGCG as 50 mM. NMR showed two binding events: strong (n1=1.8 ± 0.2; Kd1 =19 ± 12 μM) and weak (n2∼20; Kd2 =40 ± 20 mM). ITC also showed two binding events: strong (n1=2.5 ± 0.03; Kd1 =21.6 ± 4.0 μM) and weak (n2=9 ± 1; Kd2 =22 ± 4 mM). The two techniques are consistent, with an unexpectedly high number of bound EGCG. The strong binding is consistent with binding in the two Sudlow pockets. These results imply that almost all EGCG is transported in the blood bound to albumin and explains the wide tissue distribution and chemical stability of EGCG in vivo.

scholarly journals Thermodynamic Study of Human Serum Albumin upon Interaction with Ytterbium (III)

2013 ◽  
Vol 2013 ◽  
pp. 1-4 ◽  
Author(s):  
G. Rezaei Behbehani ◽  
L. Barzegar ◽  
M. K. Kiani Savad Koohi ◽  
M. Mohebbian ◽  
B. Samak Abedi ◽  
...  
Keyword(s):  
Structural Change ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Isothermal Titration Calorimetry ◽  
Titration Calorimetry ◽  
Complexation Reaction ◽  
Binding Parameters ◽  
High Concentrations ◽  
Solvation Theory

Complexation reaction between Yb3+and human serum albumin is examined using isothermal titration calorimetry (ITC). The extension solvation theory was used to reproduce the enthalpies of HAS + Yb3+interactions over the whole range of Yb3+concentrations. The binding parameters recovered from this model were attributed to the structural change of HSA. The results show that Yb3+ions bind to HSA with three equivalent affinity sites. It was found that in the high concentrations of the ytterbium ions, the HSA structure was destabilized.

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