Wyniki wyszukiwania

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Binding of harmane to human and bovine serum albumin: fluorescence and phosphorescence study

100%

Galecki K., Despotovic B., Galloway C., Ioannidis A.-G., Janani T., Nakamura Y., Oluyinka G.

Biotechnology and Food Science

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2012

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tom 76

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nr 1

2

Interaction of anesthetic supplement thiopental with human serum albumin

100%

Khan S. N., Islam B., Rajeswari M. R., Usmani H., Khan A. U.

Acta Biochimica Polonica

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2008

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tom 55

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nr 2

399-409

Thiopental (TPL) is a commonly used barbiturate anesthetic. Its binding with human serum albumin (HSA) was studied to explore the anesthetic-induced protein dysfunction. The basic binding interaction was studied by UV-absorption and fluorescence spectroscopy. An increase in the binding affinity (K) and in the number of binding sites (n) with the increasing albumin concentration was observed. The interaction was conformation-dependent and the highest for the F isomer of HSA, which implicates its slow elimination. The mode of binding was characterized using various thermodynamic parameters. Domain II of HSA was found to possess a high affinity binding site for TPL. The effect of micro-metal ions on the binding affinity was also investigated. The molecular distance, r, between donor (HSA) and acceptor (TPL) was estimated by fluorescence resonance energy transfer (FRET). Correlation between the stability of the TPL-N and TPL-F complexes and drug distribution is discussed. The structural changes in the protein investigated by circular dichroism (CD) and Fourier transform infrared (FT-IR) spectroscopy reflect perturbation of the albumin molecule and provide an explanation for the heterogeneity of action of this anesthetic.

3

The anti-apoptotic activity of albumin for endothelium is inhibited by advanced glycation and products restricting intramolecular movement

100%

Zoellner H., Siddiqui S., Kelly E., Medbury H.

Cellular and Molecular Biology Letters

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2009

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tom 14

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nr 4

575-586

Human serum albumin (HSA) inhibits endothelial apoptosis in a highly specific manner. CNBr fragmentation greatly increases the effectiveness of this activity, suggesting that this type of protection is mediated by a partially cryptic albumin domain which is transiently exposed by intramolecular movement. Advanced glycation end-product (AGE) formation in HSA greatly reduces its intra-molecular movement. This study aimed to determine if this inhibits the anti-apoptotic activity of HSA, and if such inactivation could be reversed by CNBr fragmentation. HSA-AGE was prepared by incubating HSA with glucose, and assessed using the fructosamine assay, mass spectrometry, SDS-PAGE and fluorometry. Low levels of AGE in the HSA had little effect upon its anti-apoptotic activity, but when the levels of AGE were high and the intra-molecular movement was reduced, endothelial cell survival was also found to be reduced to levels equivalent to those in cultures without HSA or serum (p > 0.001). Survival was restored by the inclusion of native HSA, despite the presence of HSA with high levels of AGE. Also, CNBr fragmentation of otherwise inactive HSA-AGE restored the anti-apoptotic activity for endothelium. Apoptosis was confirmed by DNA gel electrophoresis, transmission electron microscopy and fluorescence-activated cell sorting analysis, and there was no evidence for direct toxicity in the HSA-AGE preparations. The results are consistent with the proposed role of intra-molecular movement in exposing the anti-apoptotic domain in HSA for endothelium. The levels of AGE formation required to inhibit the anti-apoptotic activity of HSA exceeded those reported for diabetes. Nonetheless, the data from this study seems to be the first example of reduced protein function due to AGE-restricted intra-molecular movement.

4

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Molecular docking and binding interaction between psychedelic drugs and human serum albumin

80%

Khastar H., Foroughi K., Aghayan S. S., Yarmohammadi M., Jafarisani M.

BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology

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2020

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tom 101

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nr 2

5

A spectroscopic study of binding of prostacycline and its derivatives to proteins

80%

Buko V., Zavodnik I., Artsukievich A., Jeney A., Lapis K.

Current Topics in Biophysics

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1995

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tom 19

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nr 1

6

Gamijeonssibaekchulsan regulates mast cell-mediated anaphylactic reaction

80%

Moon P. D., Shin H. Y., Na H. J., Jeong H. J., Kim S. J., Um J. Y., Park R. K., Kim H. M., Hong S. H.

Acta Biochimica Polonica

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2007

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tom 54

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nr 2

Gamijeonssibaekchulsan (GJBS) is a typical Oriental medicine prescription which has been used in Korea for the treatment of allergic diseases and the development of physical strength. However, as yet there is no clear explanation of how GJBS affects the anaphylactic reaction and the immune function. In the present study murine models and MOLT-4 cells, a T cell line, were used to investigate these effects. Compound 48/80-induced systemic anaphylactic shock and ear swelling response were firstly analyzed. We also assayed histamine release and passive cutaneous anaphylaxis (PCA) in mice and cytokine productions in MOLT-4 cells. GJBS significantly inhibits compound 48/80-induced systemic anaphylactic shock and ear swelling response. GJBS also inhibits histamine release from rat peritoneal mast cells induced by compound 48/80. PCA activated by anti-dinitrophenyl immunoglobulin E is attenuated by GJBS. However, GJBS dose not affect the production of interferon-γ, interleukin (IL)-2, and IL-4 in MOLT-4 cells. These results indicate that GJBS has a potential regulatory effect on allergic reactions that are mediated by mast cells.

Ograniczanie wyników

Binding of harmane to human and bovine serum albumin: fluorescence and phosphorescence study

Interaction of anesthetic supplement thiopental with human serum albumin

The anti-apoptotic activity of albumin for endothelium is inhibited by advanced glycation and products restricting intramolecular movement

Molecular docking and binding interaction between psychedelic drugs and human serum albumin

A spectroscopic study of binding of prostacycline and its derivatives to proteins

Gamijeonssibaekchulsan regulates mast cell-mediated anaphylactic reaction