Alkylation of Human Serum Albumin by Sulfur Mustard in Vitro and in Vivo:  Mass Spectrometric Analysis of a Cysteine Adduct as a Sensitive Biomarker of Exposure

1999 ◽  
Vol 12 (8) ◽  
pp. 715-721 ◽  
Author(s):  
Daan Noort ◽  
Albert G. Hulst ◽  
Leo P. A. de Jong ◽  
Hendrik P. Benschop
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Sulfur Mustard ◽  
Mass Spectrometric ◽  
Mass Spectrometric Analysis ◽  
Spectrometric Analysis ◽  
Biomarker Of Exposure

scholarly journals Data set for mass spectrometric analysis of recombinant human serum albumin from various expression systems

Data in Brief ◽  
2015 ◽  
Vol 4 ◽  
pp. 583-586
Author(s):  
Daryl G.S. Smith ◽  
Grant E. Frahm ◽  
Anita Kane ◽  
Barry Lorbetskie ◽  
Michel Girard ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Mass Spectrometric ◽  
Mass Spectrometric Analysis ◽  
Spectrometric Analysis ◽  
Expression Systems ◽  
Data Set ◽  
Recombinant Human Serum Albumin

In vitro and in vivo antitubercular activity of benzothiazinone-loaded human serum albumin nanocarriers designed for inhalation

2020 ◽  
Vol 328 ◽  
pp. 339-349 ◽  
Author(s):  
Ayasha Patel ◽  
Natalja Redinger ◽  
Adrian Richter ◽  
Arcadia Woods ◽  
Paul Robert Neumann ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Antitubercular Activity

An effective and safe treatment strategy for rheumatoid arthritis based on human serum albumin and Kolliphor® HS 15

Nanomedicine ◽  
2019 ◽  
Vol 14 (16) ◽  
pp. 2169-2187 ◽  
Author(s):  
Ting Gong ◽  
Pei Zhang ◽  
Caifeng Deng ◽  
Yu Xiao ◽  
Tao Gong ◽  
...  
Keyword(s):  
Rheumatoid Arthritis ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Therapeutic Strategy ◽  
Inflammatory Cell ◽  
In Vivo Studies ◽  
Targeting Ability

Aim: We aimed to construct human serum albumin-Kolliphor® HS 15 nanoparticles (HSA-HS15 NPs) to overcome the limitations in targeted therapy for rheumatoid arthritis (RA) and enhance the safety of drug-loaded HSA NPs. Methodology: Celastrol (CLT)-loaded HSA-HS15 NPs were prepared and the properties were adequately investigated; the treatment effect were evaluated in RA rats; in vitro and in vivo studies were performed to explain the mechanism. Results: CLT-HSA-HS15 NPs had remarkable treatment ability and enhanced safety in the treatment of RA compared with free CLT and CLT-HSA NPs. Conclusion: HSA-HS15 NPs could be a safe and efficient therapeutic strategy for the treatment of RA, because of the inflammatory targeting ability of albumin, the added HS15 and ELVIS effect (extravasation through leaky vasculature followed by inflammatory cell-mediated sequestration) of nanoparticles.

scholarly journals Development of Meloxicam-Human Serum Albumin Nanoparticles for Nose-to-Brain Delivery via Application of a Quality by Design Approach

Pharmaceutics ◽  
2020 ◽  
Vol 12 (2) ◽  
pp. 97 ◽  
Author(s):  
Gábor Katona ◽  
György Tibor Balogh ◽  
Gergő Dargó ◽  
Róbert Gáspár ◽  
Árpád Márki ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Zeta Potential ◽  
Serum Albumin ◽  
Human Serum ◽  
Quality By Design ◽  
Tween 80 ◽  
Critical Parameters ◽  
Brain Delivery

The aim of this study was to optimize the formulation of meloxicam (MEL)-containing human serum albumin (HSA) nanoparticles for nose-to-brain via a quality by design (QbD) approach. Liquid and dried formulations of nanoparticles containing Tween 80 and without the surfactant were investigated. Various properties, such as the Z-average, zeta potential, encapsulation efficacy (EE), conjugation of MEL and HSA, physical stability, in vitro dissolution, in vitro permeability, and in vivo plasma and brain distribution of MEL were characterized. From a stability point of view, a solid product (Mel-HSA-Tween) is recommended for further development since it met the desired critical parameters (176 ± 0.3 nm Z-average, 0.205 ± 0.01 PdI, −14.1 ± 0.7 mV zeta potential) after 6 months of storage. In vitro examination showed a significantly increased drug dissolution and permeability of MEL-containing nanoparticles, especially in the case of applying Tween 80. The in vivo studies confirmed both the trans-epithelial and axonal transport of nanoparticles, and a significantly higher cerebral concentration of MEL was detected with nose-to-brain delivery, in comparison with intravenous or per os administration. These results indicate intranasal the administration of optimized MEL-containing HSA formulations as a potentially applicable “value-added” product for the treatment of neuroinflammation.

In vitro and in vivo cytotoxic activity and human serum albumin interaction for a methoxy-styryl-thiosemicarbazone

2019 ◽  
Vol 37 (5) ◽  
pp. 994-1005 ◽  
Author(s):  
Otávio Augusto Chaves ◽  
Isabela S. de Castro ◽  
Carla Marins Goulart ◽  
Myrtes S. S. Bellieny ◽  
José Carlos Netto-Ferreira ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Cytotoxic Activity

scholarly journals Human serum albumin-mediated apoptin delivery suppresses breast cancer cell growth in vitro and in vivo

2016 ◽  
Vol 13 (2) ◽  
pp. 579-586 ◽  
Author(s):  
Fang Wu ◽  
Yizhi Liu ◽  
Jian Li ◽  
Lei Hou ◽  
Fuxi Lei ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Cell Growth ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Breast Cancer Cell ◽  
Cancer Cell Growth ◽  
Breast Cancer Cell Growth

scholarly journals Absence of the CXCR4 Antagonist EPI-X4 from Pharmaceutical Human Serum Albumin Preparations

2021 ◽  
Author(s):  
Andrea Gilg ◽  
Mirja Harms ◽  
Lia-Raluca Olari ◽  
Ann-Kathrin Urbanowitz ◽  
Halvard Bonig ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Cxcr4 Antagonist ◽  
Aspartic Proteases ◽  
Cxc Chemokine Receptor 4 ◽  
High Concentrations ◽  
Chemokine Receptor 4

Background: Endogenous Peptide Inhibitor of CXCR4 (EPI-X4) is a natural antagonist of the CXC chemokine receptor 4 (CXCR4). EPI-X4 is a 16-mer peptide that is released from human serum albumin (HSA) by acidic aspartic proteases such as Cathepsin D and E. Since human serum albumin (HSA) is an important medicinal substance we asked whether different pharmaceutical HSA products contain EPI-X4 which could have been generated during manufacturing and whether HSA can serve as a substrate for cathepsins despite of the presence of stabilizers like caprylate. Methods: Eight pharmaceutical HSA preparations representing all currently used fractionation technologies were analyzed. The previously described specific EPI-X4 ELISA was used for quantification; in vitro EPI-X4 generation by acidification in the presence or absence of cathepsins was followed by quantification with ELISA. Results: None of the pharmaceutical HSA preparations tested contained EPI-X4. Acidification of HSA did not generate EPI-X4. Addition of cathepsins D and E to acidified HSA yielded high concentrations of EPI-X4 in all HSA preparations, indistinguishable between individual products. Conclusion: Medicinal HSA preparations per se do not contain EPI-X4, but will replenish its precursor which can be cleaved to EPI-X4 in vivo, environmental conditions permitting.

scholarly journals Evaluation of the in vitro Activity and in vivo Efficacy of Anidulafungin-Loaded Human Serum Albumin Nanoparticles Against Candida albicans

2021 ◽  
Vol 12 ◽  
Author(s):  
Yu Zhang ◽  
Yan-Chao Liu ◽  
Si-Min Chen ◽  
Hui Zong ◽  
Wei-Tong Hou ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Water Solubility ◽  
Fungal Infections ◽  
Antifungal Susceptibility ◽  
Fungal Species ◽  
Invasive Infection

Recent decades have seen a significant increase in invasive fungal infections, resulting in unacceptably high mortality rates. Anidulafungin (AN) is the newest echinocandin and appears to have several advantages over existing antifungals. However, its poor water solubility and burdensome route of administration (i.e., repeated, long-term intravenous infusions) have limited its practical use. The objective of this study was to develop anidulafungin-loaded Human Serum Albumin (HSA) nanoparticles (NP) so as to increase both its solubility and antifungal efficacy. HSA was reduced using SDS and DTT, allowing liberation of free thiols to form the intermolecular disulfide network and nanoassembly. Reduced HSA was then added to MES buffer (0.1 M, pH 4.8) and magnetically stirred at 350 rpm and 25°C with AN (m/m 50:1) for 2 h to form nanoparticles (AN NP). We next performed routine antifungal susceptibility testing of Candida strains (n = 31) using Clinical and Laboratory Standards Institute (CLSI) methodologies. Finally, the in vivo efficacy of both AN and AN NP was investigated in a murine model of invasive infection by one of the most common fungal species—C. albicans. The results indicated that our carrier formulations successfully improved the water solubility of AN and encapsulated AN, with the latter having a particle size of 29 ± 1.5 nm with Polymer dispersity index (PDI) equaling 0.173 ± 0.039. In vitro AN NP testing revealed a stronger effect against Candida species (n = 31), with Minimum Inhibitory Concentration (MIC) values 4- to 32-fold lower than AN alone. In mice infected with Candida and having invasive candidiasis, we found that AN NP prolonged survival time (P < 0.005) and reduced fungal burden in kidneys compared to equivalent concentrations of free drug (P < 0.0001). In conclusion, the anidulafungin nanoparticles developed here have the potential to improve drug administration and therapeutic outcomes for individuals suffering from fungal diseases.

scholarly journals A Biophysical Comparison of Human Serum Albumin to be Glycated In Vivo and In Vitro

2011 ◽  
Vol 30 (1) ◽  
pp. 5-10 ◽  
Author(s):  
Naghmeh Sattarahmady ◽  
Ali Moosavi-Movahedi ◽  
Mehran Habibi-Rezaei
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Physiological Conditions ◽  
Glycation End Products ◽  
Biophysical Studies ◽  
Arginine Residues ◽  
Glycation Process

A Biophysical Comparison of Human Serum Albumin to be GlycatedIn VivoandIn VitroThe glycation process includes the arrangement of proteins with chemically reversible early glycation products, Schiff bases and Amadori adducts. These early products endure slow and complex rearrangements to create advanced glycation end-products (AGEs) that are involved in diabetic complications. Here, the biophysical characteristics ofin vitroglycated human serum albumin (HSA) are compared to those of HSA glycatedin vivo. The changes in the content of α-helices, AGE-specific fluorescence intensity, extent of lysine residue modification, and surface tension value and also the formation of Amadori products in HSA are similar in both conditions. It was observed, however, that arginine residues were modified only under physiological conditions (in vivo), while the same did not occurin vitro. This difference was related to the presence of 3-deoxyglucosone, a 1,2-dicarbonyl compound derived from glucose under physiological conditions. Therefore, the biophysical studies on the HSA glycation processin vitroare credible.

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