Thermodynamic Characterization of Drug Binding to Human Serum Albumin by Isothermal Titration Microcalorimetry

1994 ◽  
Vol 83 (12) ◽  
pp. 1712-1716 ◽  
Author(s):  
Hatsumi Aki ◽  
Magobei Yamamoto
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Drug Binding ◽  
Thermodynamic Characterization ◽  
Isothermal Titration Microcalorimetry ◽  
Titration Microcalorimetry

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.

scholarly journals The Influence of Oxidative Stress on Serum Albumin Structure as a Carrier of Selected Diazaphenothiazine with Potential Anticancer Activity

2021 ◽  
Vol 14 (3) ◽  
pp. 285
Author(s):  
Małgorzata Maciążek-Jurczyk ◽  
Beata Morak-Młodawska ◽  
Małgorzata Jeleń ◽  
Wiktoria Kopeć ◽  
Agnieszka Szkudlarek ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Anticancer Activity ◽  
Drug Distribution ◽  
Cd Spectroscopy ◽  
Drug Binding ◽  
Protein Activity ◽  
Chloramine T ◽  
The Stability

Albumin is one of the most important proteins in human blood. Among its multiple functions, drug binding is crucial in terms of drug distribution in human body. This protein undergoes many modifications that are certain to influence protein activity and affect its structure. One such reaction is albumin oxidation. Chloramine T is a strong oxidant. Solutions of human serum albumin, both non-modified and modified by chloramine T, were examined with the use of fluorescence, absorption and circular dichroism (CD) spectroscopy. 10H-3,6-diazaphenothiazine (DAPT) has anticancer activity and it has been studied for the first time in terms of binding with human serum albumin—its potential as a transporting protein. Using fluorescence spectroscopy, in the presence of dansylated amino acids, dansyl-l-glutamine (dGlu), dansyl-l-proline (dPro), DAPT binding with two main albumin sites—in subdomain IIA and IIIA—has been evaluated. Based on the conducted data, in order to measure the stability of DAPT complexes with human (HSA) and oxidized (oHSA) serum albumin, association constant (Ka) for ligand-HSA and ligand-oHSA complexes were calculated. It has been presumed that oxidation is not an important issue in terms of 10H-3,6-diazaphenothiazine binding to albumin. It means that the distribution of this substance is similar regardless of changes in albumin structure caused by oxidation, natural occurring in the organism.

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