scholarly journals Comparison of kinetic study of the photochemical changes of (ZZ)-bilirubin IXα bound to human serum albumin with that bound to rat serum albumin

1985 ◽  
Vol 230 (3) ◽  
pp. 561-567 ◽  
Author(s):  
S Onishi ◽  
S Itoh ◽  
T Yamakawa ◽  
K Isobe ◽  
M Manabe ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Rate Constants ◽  
Relative Rate ◽  
Rat Serum ◽  
Relative Rate Constants ◽  
Rat Serum Albumin

It has been stated by McDonagh, Palma & Lightner [(1982) J. Am. Chem. Soc. 104, 6867-6871] that complexing of bilirubin with serum albumin has a marked species-dependent influence on bilirubin photoisomerization in vitro and in vivo. Therefore the kinetics for the quantitatively important reaction: (Formula: see text) of the photochemical interconversion between bilirubin and its photoisomers bound to human or rat serum albumin in aqueous solution, assayed by h.p.l.c., was used to elucidate the observed species-dependent difference. The relative rate constants for bilirubin bound to human serum albumin, except for k4, the rate of interconversion from (ZZ)-bilirubin into (EZ)-bilirubin, proved to be considerably larger than those for bilirubin bound to rat serum albumin. In accordance with these rate constants, the formation of photoisomers of bilirubin bound to human serum albumin, except for (EZ)-bilirubin, is very rapid and much greater than that for bilirubin bound to rat serum albumin.

scholarly journals Wavelength-dependence of the relative rate constants for the main geometric and structural photoisomerization of bilirubin IX α bound to human serum albumin. Demonstration of green light at 510 nm as the most effective wavelength in photochemical changes from (ZZ)-bilirubin IX α to (EZ)-cyclobilirubin IX α via (EZ)-bilirubin

1986 ◽  
Vol 236 (1) ◽  
pp. 23-29 ◽  
Author(s):  
S Onishi ◽  
S Itoh ◽  
K Isobe
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Light Source ◽  
Rate Constants ◽  
Relative Rate ◽  
Green Light ◽  
Wavelength Dependence ◽  
Relative Rate Constants

The kinetics for the quantitatively important reaction: (Formula: see text) that is, the photochemical interconversion between bilirubin and its geometric and structural photoisomers bound to human serum albumin in aqueous solution when various wavelengths of monochromatic light were used, were assayed by h.p.l.c. In order to clarify the wavelength-dependence of the relative rate constants in the individual steps, a light-source with a half-bandwidth of 10 nm was used at increments of 20 nm, in the range from 410 nm to 550 nm. We describe for the first time studies on the wavelength-dependence of rate constants in geometric and structural photoisomerization reactions in vitro of (ZZ)-bilirubin or (EZ)-bilirubin bound to human serum albumin, especially the relative rate constants of cyclization of (EZ)-bilirubin into (EZ)-cyclobilirubin. Because studies in vitro have demonstrated that the wavelengths from 350 to 450 nm are mutagenic, the results obtained indicated that the safest and ideal light-source for phototherapy is green light of 510 nm, which keeps (ZE)-bilirubin concentrations as low as possible, as shown by a maximal value of k2 at 510 nm and a relatively low value of k1 at 510 nm. This light-source still ensures the substantial absorption of (ZZ)-bilirubin, which is the precursor of (EZ)-bilirubin, the intermediate in (EZ)-cyclobilirubin formation and, furthermore, as shown by the maximal value of k5 and a considerable value of k4 at 510 nm, promotes the cyclization of (EZ)-bilirubin derived from (ZZ)-bilirubin even though k3 at 510 nm also shows a peak value.

scholarly journals Kinetic study of the photochemical changes of (ZZ)-bilirubin IX α bound to human serum albumin. Demonstration of (EZ)-bilirubin IX α as an intermediate in photochemical changes from (ZZ)-bilirubin IX α to (EZ)-cyclobilirubin IX α

1985 ◽  
Vol 226 (1) ◽  
pp. 251-258 ◽  
Author(s):  
S Itoh ◽  
S Onishi
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Kinetic Study ◽  
Human Serum ◽  
Photochemical Reaction ◽  
Relative Rate ◽  
Significant Preference ◽  
Geometrical Isomers ◽  
Relative Rate Constants

The present study was performed to elucidate why the photochemical reaction of (ZZ)-bilirubin bound to human serum albumin is singularly selective, and only one of the two (EZ)- and (ZE)-bilirubins, the (ZE)-isomer, is produced. In a kinetic study of the photochemical reaction in vitro, the sum of the relative rate constants of photochemical transformation of (EZ)-bilirubin into both (EZ)-cyclobilirubin and (ZZ)-bilirubin, with a significant preference for the former, was proved to be considerably larger than that of the transformation of (ZZ)-bilirubin into (EZ)-bilirubin. Therefore only one of the geometrical isomers, namely (ZE)-bilirubin, is apparently formed. It was concluded that (EZ)-bilirubin photochemically undergoes (EZ)-cyclization, i.e. structural photoisomerization, while bound to its high-affinity site on human serum albumin, and is an intermediate in the transformation of (ZZ)-bilirubin into (EZ)-cyclobilirubin.

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.

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