STUDY OF INTERACTION OF HOECHST 33258 WITH DNA AND HUMAN SERUM ALBUMIN UNDER THE INFLUENCE OF MILLIMETER RANGE ELECTROMAGNETIC WAVES

2021 ◽  
Vol 55 (2 (255)) ◽  
pp. 136-143
Author(s):  
Poghos H. Vardevanyan ◽  
Mariam A. Shahinyan ◽  
Anna V. Vardanyan ◽  
Svetlana V. Grigoryan
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Electromagnetic Waves ◽  
Binding Constants ◽  
Hoechst 33258

In this work the effect of millimeter range electromagnetic waves (MM EMW) with the frequency 64.5 GHz on the complexes of Hoechst 33258 (H33258) with DNA and human serum albumin (HSA) has been studied by the methods of absorption and fluorescence spectroscopies. It was shown that the irradiation results in weakening of H33258 interaction with both macromolecules, which is connected with the fact that the frequency 64.5 GHz, being resonant for water, leads to the structurizing of water component around DNA and HSA, due to which the binding becomes weaker. This conclusion is based on the values of both binding constants and Stern–Volmer constants.

Study of the influence of millimeter range electromagnetic waves on methylene blue complexes with human serum albumin

2019 ◽  
Vol 33 (17) ◽  
pp. 2317-2327
Author(s):  
Mariam A. Shahinyan ◽  
Ara P. Antonyan ◽  
Vitali P. Kalantaryan ◽  
Marieta S. Mikaelyan ◽  
Poghos O. Vardevanyan
Keyword(s):  
Methylene Blue ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Electromagnetic Waves

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.

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.

scholarly journals Deuteroporphyrin-albumin binding equilibrium. The effects of porphyrin self-aggregation studied for the human and the bovine proteins

1985 ◽  
Vol 229 (1) ◽  
pp. 197-203 ◽  
Author(s):  
M Rotenberg ◽  
R Margalit
Keyword(s):  
Human Serum Albumin ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Bovine Serum ◽  
Binding Constants ◽  
Protein Molecule ◽  
Competitive Model ◽  
Phosphate Buffered Saline ◽  
Self Aggregation

The binding equilibrium of deuteroporphyrin IX to human serum albumin and to bovine serum albumin was studied, by monitoring protein-induced changes in the porphyrin fluorescence and taking into consideration the self-aggregation of the porphyrin. To have control over the latter, the range of porphyrin concentrations was chosen to maker dimers (non-covalent) the dominant aggregate. Each protein was found to have one high-affinity site for deuteroporphyrin IX monomers, the magnitudes of the equilibrium binding constants (25 degrees C, neutral pH, phosphate-buffered saline) being 4.5 (+/- 1.5) X 10(7) M-1 and 1.7 (+/- 0.2) X 10(6) M-1 for human serum albumin and for bovine serum albumin respectively. Deuteroporphyrin IX dimers were found to bind directly to the protein, each protein binding one dimer, with high affinity. Two models are proposed for the protein-binding of porphyrin monomers and dimers in a porphyrin system having both species: a competitive model, where each protein molecule has only one binding site, which can be occupied by either a monomer or a dimer; a non-competitive model, where each protein molecule has two binding sites, one for monomers and one for dimers. On testing the fit of the data to the models, an argument can be made to favour the non-competitive model, the equilibrium binding constants of the dimers, for the non-competitive model (25 degrees C, neutral pH, phosphate-buffered saline), being: 8.0 (+/- 1.8) X 10(8) M-1 and 1.2 (+/- 0.6) X 10(7) M-1 for human serum albumin and bovine serum albumin respectively.

scholarly journals Molecular mechanistic vision on binding interaction of triptan drug, a serotonin (5-HT1) agonist with human serum albumin through multispectral and computational assessments

2020 ◽  
Vol 11 (2) ◽  
pp. 145-155
Author(s):  
Manjushree Makegowda ◽  
Revanasiddappa Hosakere Doddarevanna
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Clinical Medicine ◽  
Fluorescence Emission ◽  
Binding Constants ◽  
Binding Interaction ◽  
Binding Ability ◽  
Ft Ir ◽  
Ft Ir Spectroscopy

The triptan drug such as eletriptan in combination with hydrochloride (ETP) is a 5-HT1 receptor agonist used to treat the migraine headache. Human serum albumin (HSA), the fundamental serum protein, executes various functions, that includes transporting and binding of many ligands. HSA binding interaction with ETP is elucidated from molecular docking in composite with fluorescence (emission, 3D and synchronous), UV-vis and FT-IR spectroscopy at 296, 304 and 312 K (pH = 7.40). ETP after interaction modified the HSA secondary structure and its micro-environments. Energy transfer and thermodynamic parameters were evaluated. Various quenching and binding constants were computed for formed ETP-HSA complex. The dominant interactive forces for ETP and HSA binding are hydrogen bonds join up with van der Waals extent possibly at site III (IB). The presence of Ca2+, Co2+, Na+, Mg2+ and Fe3+ ions significantly affected binding ability of ETP towards HSA. The essentialness of this investigation is beneficial in life sciences, medicinal chemistry, pharmaceutical industry and clinical medicine.

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