Kinetic and thermodynamic characterization of camptothecin hydrolysis at physiological pH in the absence and presence of human serum albumin

2009 ◽  
Vol 41 (11) ◽  
pp. 704-715 ◽  
Author(s):  
Rishi Thakur ◽  
Sasank Kunadharaju ◽  
Michalakis Savva
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Thermodynamic Characterization

scholarly journals Thermodynamic characterization of phthalocyanine–human serum albumin interaction

2011 ◽  
Vol 25 (5) ◽  
pp. 235-242 ◽  
Author(s):  
Hamid Dezhampanah ◽  
Abdol Khalegh Bordbar ◽  
Shamim Farshad
Keyword(s):  
Human Serum Albumin ◽  
Optical Absorption ◽  
Serum Albumin ◽  
Human Serum ◽  
Optical Absorption Spectroscopy ◽  
Thermodynamic Characterization ◽  
Enthalpy And Entropy Changes ◽  
Enthalpy And Entropy ◽  
Hoff Equation

The thermodynamic of the binding of nickel (II) tetrasulfonated phthalocyanine anion [Ni(tspc)4–], to human serum albumin (HSA) was investigated in 5 mM aqueous phosphate buffer of pH 7.40 at 25°C using optical absorption spectroscopy. The results show that [Ni(tspc)4–] does not have any affinity for aggregation due to increasing of salt concentration and exists as monomers even in homogeneous aqueous solutions of high ionic strengths (more than 2 M NaCl). The binding constant (K) was obtained by analysis of optical absorption spectra of mentioned complex at various HSA concentrations using SQUAD software. The value ofKwas estimated to be 4.89×105±0.03 (M–1) at 25°C. The thermodynamic parameters were calculated by van’t Hoff equation. The enthalpy and entropy changes were 28.08 kJ/mol and 203.09 J/(mol?·?K) at 25°C, respectively. The results indicate that the binding is mainly entropy driven and the enthalpy is unfavorable for it, the hydrophobic forces thus playing a major role in the binding process.

scholarly journals Characterization of the Solution Structure of Human Serum Albumin Loaded with a Metal Porphyrin and Fatty Acids

2011 ◽  
Vol 100 (9) ◽  
pp. 2293-2301 ◽  
Author(s):  
Matthias J.N. Junk ◽  
Hans W. Spiess ◽  
Dariush Hinderberger
Keyword(s):  
Fatty Acids ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Solution Structure ◽  
Metal Porphyrin

Highly precise characterization of the hydration state upon thermal denaturation of human serum albumin using a 65 GHz dielectric sensor

2020 ◽  
Vol 22 (35) ◽  
pp. 19468-19479 ◽  
Author(s):  
Keiichiro Shiraga ◽  
Mako Urabe ◽  
Takeshi Matsui ◽  
Shojiro Kikuchi ◽  
Yuichi Ogawa
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Thermal Denaturation ◽  
Hydration Water ◽  
Biological Functions ◽  
Dielectric Sensor ◽  
Hydration State ◽  
Precise Characterization

The biological functions of proteins depend on harmonization with hydration water surrounding them.

Sign in / Sign up

Export Citation Format

Share Document