scholarly journals Synthesis and Comparative Study of Nanoparticles Derived from Bovine and Human Serum Albumins

Polymers ◽  
2020 ◽  
Vol 12 (6) ◽  
pp. 1301 ◽  
Author(s):  
Yerkeblan Tazhbayev ◽  
Olzhas Mukashev ◽  
Meiram Burkeyev ◽  
Vladimir I. Lozinsky
Keyword(s):  
Human Serum Albumin ◽  
Bovine Serum Albumin ◽  
Drug Release ◽  
Serum Albumin ◽  
Human Serum ◽  
Release Profile ◽  
Serum Albumins ◽  
Drug Release Profile ◽  
Protein Nanoparticles ◽  
Inclusion Methods

This study describes the preparation of nanoparticles derived from bovine serum albumin (BSA) in comparison with the formation of nanoparticles composed of human serum albumin (HSA), when the same preparation procedure was used in both cases. To obtain protein nanoparticles, the method of desolvation with ethanol was employed, followed by the stabilization with urea and cysteine. It was shown that, upon transition from HSA to BSA, the particles with smaller sizes and with a narrower polydispersity were formed. The possibility of the immobilization of the antitumor drug hydroxyurea in such protein nanoparticles by adsorption and inclusion methods has been shown. The drug release profile from the polymer matrix was established.

Interaction of 4-Nitroaniline with Serum Albumin

2014 ◽  
Vol 522-524 ◽  
pp. 337-340
Author(s):  
Yan Qiu Liang ◽  
Ying Zhang
Keyword(s):  
Hydrogen Bond ◽  
Human Serum Albumin ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Constants ◽  
Positive Entropy ◽  
Serum Albumins ◽  
High Affinity ◽  
Tryptophan Residues

Bovine serum albumin (BSA) and human serum albumin (HSA) interaction with 4-nitroaniline was investigated by fluorescence spectroscopy respectively. 4-Nitroaniline can strongly quench intrinsic fluorescence of BSA and HSA. 4-Nitroaniline exhibits a high affinity to bovine and human serum albumins. The binding constantsKand the number binding sitenwere obtained by double-log regression equation. Negative enthalpy (ΔH) and positive entropy (ΔS) values indicated that both hydrogen bond and hydrophobic forces played a major role in the binding of 4-nitroaniline and SA. The results of synchronous fluorescence showed the polarity around tryptophan residues was decreased and the hydrophobicity was increased.

Serum Albumins Guided Plasmonic Nanoassemblies with Opposite Chiralities

Soft Matter ◽  
2021 ◽  
Author(s):  
Zhaoyi Wang ◽  
Ningning Zhang ◽  
Jincheng Li ◽  
Jun Lu ◽  
Li Zhao ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Great Promise ◽  
Plasmonic Nanostructures ◽  
Serum Albumins ◽  
Catalytic Applications

Chiral assemblies by combining natural biomolecules with plasmonic nanostructures hold great promise for plasmonic enhanced sensing, imaging, and catalytic applications. Herein, we demonstrate that human serum albumin (HSA) and porcine...

scholarly journals IMMUNOLOGIC TOLERANCE AFTER SPECIFIC IMMUNIZATION

1964 ◽  
Vol 120 (3) ◽  
pp. 435-447 ◽  
Author(s):  
Marianne M. Dorner ◽  
Jonathan W. Uhr
Keyword(s):  
Human Serum Albumin ◽  
Bovine Serum Albumin ◽  
Antibody Response ◽  
Serum Albumin ◽  
Human Serum ◽  
Bovine Serum ◽  
The State ◽  
Immunologic Tolerance ◽  
Secondary Antibody

Specific immunologic tolerance to bovine serum albumin (BSA) was induced in approximately one-half of the rabbits that had been primarily immunized and were prepared for a secondary antibody response to BSA. The state of tolerance lasted for several months in the majority of rabbits and was not easily terminated by immunization with human serum albumin followed by BSA.

scholarly journals Spectroscopic and molecular docking studies reveal binding characteristics of nazartinib (EGF816) to human serum albumin

2020 ◽  
Vol 7 (1) ◽  
pp. 191595 ◽  
Author(s):  
Abdulrahman A. Almehizia ◽  
Haitham AlRabiah ◽  
Ahmed H. Bakheit ◽  
Eman S. G. Hassan ◽  
Rashed N. Herqash ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Kinase Inhibitor ◽  
Electrostatic Force ◽  
Total Binding Energy ◽  
Serum Albumins ◽  
Binding Characteristics ◽  
Theoretical Approaches ◽  
Anti Cancer

The interactions of novel anti-cancer therapeutic agents with the different plasma and tissue components, specifically serum albumins, have lately gained considerable attention due to the significant influence of such interactions on the pharmacokinetics and/or -dynamics of this important class of therapeutics. Nazartinib (EGF 816; NAZ) is a new anti-cancer candidate proposed as a third-generation epidermal growth factor receptor tyrosine kinase inhibitor that is being developed and clinically tested for the management of non-small cell lung cancer. The current study aimed to characterize the interaction between NAZ and human serum albumin (HSA) using experimental and theoretical approaches. Experimental results of fluorescence quenching of HSA induced by NAZ revealed the development of a statically formed complex between NAZ and HSA. Interpretation of the observed fluorescence data using Stern–Volmer, Lineweaver–Burk and double-log formulae resulted in binding constants for HSA-NAZ complex in the range of (2.34–2.81) × 10 4 M –1 over the studied temperatures. These computed values were further used to elucidate thermodynamic attributes of the interaction, which showed that NAZ spontaneously binds to HSA with a postulated electrostatic force-driven interaction. This was further verified by theoretical examination of the NAZ docking on the HSA surface that revealed an HSA-NAZ complex where NAZ is bound to HSA Sudlow site I driven by hydrogen bonding in addition to electrostatic forces in the form of pi-H bond. The HSA binding pocket for NAZ was shown to encompass ARG 257, ARG 222, LYS 199 and GLU 292 with a total binding energy of −25.59 kJ mol –1 .

Glycylglycylglycine as a Synthetic Standard for Serum Protein Determination

1974 ◽  
Vol 20 (1) ◽  
pp. 70-73
Author(s):  
Bernard Klein
Keyword(s):  
Human Serum Albumin ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Serum Protein ◽  
Bovine Serum ◽  
Molar Absorptivity ◽  
Protein Determination ◽  
Synthetic Standard ◽  
Mean Differences

Abstract Glycylglycylglycine was investigated as a reference standard for use in serum protein measurement by the biuret reaction. The tripeptide-biuret solution has a molar absorptivity of 96 at 565 nm, and absorbances at both 550 nm and 565 nm are proportional to concentration. By a manual reference procedure, the 550-nm absorbance of 1.0 g of tripeptide was equivalent to that given by 1.72 ± 0.03 g of human serum albumin or 1.43 ± 0.03 g of bovine serum albumin. By the Technicon N14b automated procedure, the absorbance of 1.0 g of tripeptide at 550 nm was equivalent to that of 1.81 ± 0.02 g of human serum albumin or 1.89 ± 0.03 g of bovine serum albumin. Results for serum protein analyses over the range 4.0 to 9.0 g/dl, when tripeptide or serum albumin was used to prepare calibration curves, showed mean differences of 0.15 g/dl in the manual mode and 0.08 g/dl in the automated mode.

scholarly journals The effect of ligand presaturation on the interaction of serum albumins with an immobilized Cibacron Blue 3G-A studied by affinity gel electrophoresis

1981 ◽  
Vol 199 (3) ◽  
pp. 465-472 ◽  
Author(s):  
E C Metcalf ◽  
B Crow ◽  
P D G Dean
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Dissociation Constant ◽  
Gel Electrophoresis ◽  
Dissociation Constants ◽  
Serum Albumins ◽  
Albumin Ratio ◽  
Cibacron Blue ◽  
Affinity Gel Electrophoresis

The interaction of the immobilized triazine dye Cibacron Blue 3G-A with rat, rabbit, sheep, goat, bovine and human serum albumins was studied by affinity gel electrophoresis. Dissociation constants were estimated in each instance and showed human serum albumin to have a significantly higher affinity for the dye than did albumin from any other species. Pretreatment of the defatted proteins with bilirubin (3 mol of bilirubin/mol of protein) did not increase the dissociation constants of the serum albumins, whereas pretreatment with palmitate (7 mol of palmitate/mol of protein) increased the dissociation constant in all cases: 3-fold for human serum albumin, 15-fold for other serum albumins. Increasing the bilirubin/albumin ratio (to 7:1) did not affect the dissociation constant of the albumins studied. Decreasing the palmitate/albumin ratio decreased the dissociation constant for human serum albumin, but did not affect those of bovine and rat albumins. Altering the chain length of the presaturating fatty acid dramatically changed the dissociation constant of both human and bovine serum albumins. Butyrate, hexanoate, octanoate and decanoate did not significantly influence the dissociation constants of bovine and human serum albumins for Cibacron Blue, whereas laurate, myristate and palmitate greatly increased the dissociation constant. These data are discussed in relationship to the behaviour of albumins during dye--agarose column chromatography. In Addendum the effect of nucleotide presaturation on the interaction between Bacillus stearothermophilus 6-phosphogluconate dehydrogenase and the immobilized triazine dyes Cibacron Blue 3G-A and Procion Red HE-3B was examined, and the implications for dye--ligand chromatography are discussed.

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