Seleno-Auranofin (Et3PAuSe-tagl): Synthesis, Spectroscopic (EXAFS,197Au Mössbauer,31P,1H,13C, and77Se NMR, ESI-MS) Characterization, Biological Activity, and Rapid Serum Albumin-Induced Triethylphosphine Oxide Generation

2010 ◽  
Vol 49 (17) ◽  
pp. 7663-7675 ◽  
Author(s):  
David T. Hill ◽  
Anvarhusein A. Isab ◽  
Don E. Griswold ◽  
Michael J. DiMartino ◽  
Elizabeth D. Matz ◽  
...  
Keyword(s):  
Biological Activity ◽  
Serum Albumin ◽  
Esi Ms ◽  
Triethylphosphine Oxide

scholarly journals Adsorption of bovine serum albumin (BSA) by bare magnetite nanoparticles with surface oxidative impurities that prevent aggregation

2019 ◽  
Vol 97 (8) ◽  
pp. 577-583 ◽  
Author(s):  
Somayeh Rahdar ◽  
Abbas Rahdar ◽  
Shahin Ahmadi ◽  
John F. Trant
Keyword(s):  
Biological Activity ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Magnetite Nanoparticles ◽  
Bovine Serum ◽  
Mammalian Cells ◽  
Particle Diameter ◽  
Resistant Bacteria ◽  
Maximum Adsorption Capacity ◽  
Corona Formation

Bare, uncoated magnetite nanoparticles, synthesized using an electrochemical surfactant-free synthesis, have highly oxidized surfaces that prevent aggregation. These particles have demonstrated highly intriguing biological activity showing extremely potent antibiotic activity against both gram-positive and gram-negative bacteria with little toxicity to rats. This difference in activity could be ascribed to the nature of the protein corona. The kinetics and thermodynamics of the binding of bovine serum albumin (BSA), used as a model serum protein, to these magnetite nanoparticles were analyzed. There is no significant change in particle diameter by dynamic light scattering following adsorption, indicating corona formation does not induce aggregation. The maximum adsorption capacity of the particles was determined to be 300 mg of BSA per gram of magnetite. The particles are able to adsorb 90% of the BSA at protein concentrations as high as 500 mg/L. The adsorption is best described using a pseudo second order model and a Langmuir Type III isotherm model. Thermodynamic analysis showed that the process is entropically driven and is spontaneous at all tested temperatures and conditions. However, it appears to be a weak to moderate physical adsorption. This moderate binding affinity could indicate the differential biological activity of these particles towards bacteria and mammalian cells and further support the contention that these are potentially useful new tools for targeting antibiotic-resistant bacteria.

Separation of human serum albumin components by RP-HPLC and CZE and their characterization by ESI-MS

1999 ◽  
Vol 49 (S1) ◽  
pp. S21-S27 ◽  
Author(s):  
M. Girard ◽  
T. Cyr ◽  
N. Mousseau ◽  
J. -C. Ethier
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Esi Ms ◽  
Rp Hplc

scholarly journals Positive and negative nano-electrospray mass spectrometry of ruthenated serum albumin supported by docking studies: an integrated approach towards defining metallodrug binding sites on proteins

Metallomics ◽  
2018 ◽  
Vol 10 (4) ◽  
pp. 587-594 ◽  
Author(s):  
Marija Nišavić ◽  
Goran V. Janjić ◽  
Amela Hozić ◽  
Marijana Petković ◽  
Miloš K. Milčić ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Serum Albumin ◽  
Binding Sites ◽  
Electrospray Mass Spectrometry ◽  
Integrated Approach ◽  
Docking Studies ◽  
Esi Ms ◽  
Negative Mode

Negative mode nanoLC/nano ESI MS was used for determing Ru(ii) binding sites on protein.

Influence of the binding of reduced NAMI-A to human serum albumin on the pharmacokinetics and biological activity

2015 ◽  
Vol 44 (4) ◽  
pp. 1905-1913 ◽  
Author(s):  
V. Novohradský ◽  
A. Bergamo ◽  
M. Cocchietto ◽  
J. Zajac ◽  
V. Brabec ◽  
...  
Keyword(s):  
Biological Activity ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Chemical Transformations

Chemical transformations of NAMI-A in biological environments.

Studies on the synthesis, characterization, human serum albumin binding and biological activity of single chain surfactant-cobalt(III) complexes

Luminescence ◽  
2015 ◽  
Vol 31 (2) ◽  
pp. 523-532 ◽  
Author(s):  
G. Vignesh ◽  
K. Sugumar ◽  
S. Arunachalam ◽  
S. Vignesh ◽  
R. Arthur James ◽  
...  
Keyword(s):  
Biological Activity ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Albumin Binding ◽  
Single Chain ◽  
Human Serum Albumin Binding
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