Aggregation behaviour of human serum albumin-carrying latex particles and binding constants of divalent cations to the latex particles

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.

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

Journal of Chemical Research ◽

10.1177/1747519819895710 ◽

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.

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

Biochemical Journal ◽

10.1042/bj2290197 ◽

1985 ◽

Vol 229 (1) ◽

pp. 197-203 ◽

Cited By ~ 31

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.

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

European Journal of Chemistry ◽

10.5155/eurjchem.11.2.145-155.1971 ◽

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

Asian Journal of Applied Chemistry Research ◽

10.9734/ajacr/2019/v4i330113 ◽

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.

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Evaluation of Drug/Ligand Binding Constants for Human Serum Albumin Using Differential Scanning Calorimetry

10.1101/2021.01.22.427858 ◽

2021 ◽

Author(s):

Matthew W. Eskew ◽

Albert S. Benight

Keyword(s):

Differential Scanning Calorimetry ◽

Human Serum Albumin ◽

Ligand Binding ◽

Serum Albumin ◽

Human Serum ◽

Dose Response ◽

Binding Constants ◽

Response Curves ◽

Scanning Calorimetry ◽

Dose Response Curves

ABSTRACTThis paper reports utilization of differential scanning calorimetry measurements to evaluate binding constants for Human Serum Albumin of 28 different drug ligands. Protein/ligand mixtures were prepared at various ligand concentrations and subjected to thermal denaturation analysis by calorimetry. From the measurements, the melting temperature, Tm, and free-energy ΔGcal(37°C) for melting ligand-bound Albumin were evaluated as a function of ligand concentration. Concentration dependent behaviors of ΔGcal(37°C) and Tm derived from protein/ligand mixtures were used to construct dose-response curves. Model fits of dose-response curves yielded quantitative evaluation of the ligand binding constant, KD, and semi-quantitative estimates of the binding stoichiometry, n. Many of the ligands had known binding affinity for Albumin with binding constants reported in the literature. Evaluated Albumin binding parameters for the ligands impressively agreed with reported literature values determined using other standard experimental methods. These results demonstrated utility of our calorimetry-based process for applications in pre-clinical drug screening.

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Immobilized replicates of sequence 136–148 of human serum albumin as adsorbents for bilirubin

Canadian Journal of Chemistry ◽

10.1139/v87-322 ◽

1987 ◽

Vol 65 (8) ◽

pp. 1927-1934 ◽

Cited By ~ 10

Author(s):

M. Bouvier ◽

G. R. Brown ◽

L. E. St-Pierre

Keyword(s):

Human Serum Albumin ◽

Serum Albumin ◽

Human Serum ◽

Solid Phase ◽

Solid Phase Peptide Synthesis ◽

Phosphate Buffer Solution ◽

Binding Constants ◽

Buffer Solution ◽

A Site ◽

Scatchard Plots

Strategic peptide sequences, patterned on the sequence 136–148 of the primary structure of human serum albumin, have been immobilized on a cross-linked polyacrylamide support using the solid phase peptide synthesis technique. Certain of the resulting materials proved to be efficient adsorbents for bilirubin from aqueous phosphate buffer solution. Amino acids such as lysine and arginine favour the binding of the ligand, whereas glutamic acid reduces it markedly. From Scatchard plots, first and second equilibrium binding constants, in the range of (0.3–9.6) × 104 M−1, were obtained using a site treatment. These binding constants are comparable to that for the binding of bilirubin by a larger fragment of bovine serum albumin that contains the synthesized sequence.

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