scholarly journals Biophysical Study for the Interactions of Some Diazo Dyes with Human Serum Albumin

2019 ◽  
pp. 1-10
Author(s):  
Mohammed Hadi Al–Douh ◽  
Elham Abdalrahem Bin Selim ◽  
Edrees Muhammad Tahir ◽  
Sabah Ahmed Abdo Esmail ◽  
Yaman Ahmed Naji ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Active Site ◽  
Essential Role ◽  
Binding Constants ◽  
Biophysical Study ◽  
Diazo Dye ◽  
Biophysical Interactions ◽  
Diazo Dyes

The biophysical interactions between the human serum albumin HSA and three synthesized diazo dyes 1-3 have been investigated by thermodynamic parameters and molecular docking technique. The binding constants Kb were calculated and the compounds were ranked according to their docking free energy. Different interactions were elucidated at the active site of the protein. Among these interactions is the hydrogen bonding which plays an essential role in the interaction with the protein. Both the theoretical and practical studies have agreed that diazo dye 1 has the strongest interaction with the active site.

Interaction of biocompatible natural rosin-based surfactants with human serum albumin: A biophysical study

2015 ◽  
Vol 167 ◽  
pp. 399-407 ◽  
Author(s):  
Mohd Ishtikhar ◽  
Mohd. Sajid Ali ◽  
Ayman M. Atta ◽  
H.A. Al-Lohedan ◽  
Lokesh Nigam ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Biophysical Study

Interactions of Poly(amidoamine) Dendrimers with Human Serum Albumin: Binding Constants and Mechanisms

ACS Nano ◽  
2011 ◽  
Vol 5 (5) ◽  
pp. 3456-3468 ◽  
Author(s):  
Jyotsnendu Giri ◽  
Mamadou S. Diallo ◽  
André J. Simpson ◽  
Yi Liu ◽  
William A. Goddard ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Constants ◽  
Albumin Binding ◽  
Human Serum Albumin Binding

scholarly journals Interaction studies of chiral non-steroidal anti-inflammatory drugs with HSA protein using capillary electrophoresis frontal analysis and electrokinetic chromatography

2015 ◽  
Author(s):  
◽  
Sinegugu Khulu
Keyword(s):  
Capillary Electrophoresis ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Constants ◽  
Binding Energies ◽  
Frontal Analysis ◽  
Drug Concentrations ◽  
Inflammatory Drugs ◽  
Anti Inflammatory

Human Serum Albumin (HSA) predominantly found in the blood plasma proteins, acts as a carrier for many drugs. In the present work binding interactions of eight arylpropionate non-steroidal anti-inflammatory drugs (NSAIDs) were studied with Human Serum Albumin HSA using Capillary Electrophoresis (CE) under physiological conditions. The concentration of HSA was kept constant (525 μM) whereas the drug concentrations were varied between 50-300 μM in each case. The Frontal analysis (FA) and Capillary Zone Electrophoresis (CZE) modes of CE were applied together with a mathematical modelling of the experimental results with a view to obtaining pharmacokinetic properties of each drug. The binding order of the drugs to HSA were established with the three methods together with the mathematical approach. Our studies revealed the presence of more than one binding sites for some of the available drugs. Additionally, molecular docking studies were conducted to establish the binding conformations of drugs in the binding pocket of the HSA. A very good correlation between the computed binding energies (docking) and the experimental binding constants were observed throughout this study. The logK values for all eight drugs were ranging from 3.37 - 4.56 for FA, 3.16 – 4.39 for CZE, and 3.48 – 5.30 for computational studies.

Biophysical Study on the Interaction between Eperisone Hydrochloride and Human Serum Albumin Using Spectroscopic, Calorimetric, and Molecular Docking Analyses

2017 ◽  
Vol 14 (5) ◽  
pp. 1656-1665 ◽  
Author(s):  
Gulam Rabbani ◽  
Mohammad Hassan Baig ◽  
Eun Ju Lee ◽  
Won-Kyung Cho ◽  
Jin Yeul Ma ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Biophysical Study

scholarly journals A study on human serum albumin corona formed on photoluminescent carbon dots

2020 ◽  
Vol 44 (7-8) ◽  
pp. 447-452
Author(s):  
Peng Wang ◽  
Ming Yuan ◽  
Na Li ◽  
Feng Zhang
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Carbon Dots ◽  
Resonance Energy ◽  
Binding Constants ◽  
Protein Corona ◽  
Hybrid Nanomaterial ◽  
Corona Formation ◽  
Biomedical Field

Fluorescence nanostructures have been widely applied in the biomedical field as therapeutic agents and as novel tools for labeling, imaging, and sensing. However, the protein corona will dramatically influence the predesigned properties of nanostructures in serum. Therefore, it is important to understand the mechanism of protein corona formation on nanostructures. Photoluminescent carbon dots have been widely applied in the biomedical field since their discovery. Due to the large overlap between the absorption spectra of proteins and the fluorescence spectra of photoluminescent carbon dots, herein we investigate the mechanism of human serum albumin corona formed on photoluminescent carbon dots using fluorescence resonance energy transfer. By employing spectroscopic methods, the binding constants and the number of binding sites between human serum albumin and photoluminescent carbon dots have been determined, and the corresponding thermodynamics are also discussed as well for the interaction between photoluminescent carbon dots and human serum albumin. In addition, we successfully demonstrate the photoluminescent carbon dots in labeling bean sprouts. We believe that the current research cannot shed light on the mechanism of protein corona formation on nanostructures, but also could benefit the design of hybrid nanomaterial which will be applied to serum environments.

Sign in / Sign up

Export Citation Format

Share Document