Activation of Thiol-Dependent Antioxidant Activity of Human Serum Albumin by Alkaline pH Is Due to the B-like Conformational Change

2000 ◽  
Vol 380 (2) ◽  
pp. 309-318 ◽  
Author(s):  
Heeyong Lee ◽  
Mee-Kyung Cha ◽  
Il-Han Kim
Keyword(s):  
Antioxidant Activity ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Conformational Change ◽  
Alkaline Ph

FLUORESCENCE CHANGE OF HUMAN SERUM ALBUMIN INDUCED BY METHYL VIOLET

2020 ◽  
Vol 54 (3 (253)) ◽  
pp. 261-264
Author(s):  
M.A. Shahinyan ◽  
N.H. Petrosyan ◽  
A.P. Antonyan
Keyword(s):  
Human Serum Albumin ◽  
Fluorescence Spectroscopy ◽  
Serum Albumin ◽  
Human Serum ◽  
Conformational Change ◽  
Fluorescence Intensity ◽  
Methyl Violet ◽  
Spectroscopy Method ◽  
Intensity Maximum ◽  
Fluorescence Change

The interaction of methyl violet (MV) with human serum albumin (HSA) has been studied, using the fluorescence spectroscopy method. It was shown that MV chnages the own fluorescence of HSA. It was also shown that MV does not induce any conformational change in the structure of HSA, since there is no change of the wavelength of HSA fluorescence intensity maximum. MV binds to HSA, near to fluorescing tryptophan, which in the hydrophilic environment, and changes the own fluorescence of the protein.

Biophysical investigation of thymoquinone binding to ‘N’ and ‘B’ isoforms of human serum albumin: exploring the interaction mechanism and radical scavenging activity

RSC Advances ◽  
2015 ◽  
Vol 5 (24) ◽  
pp. 18218-18232 ◽  
Author(s):  
Mohd Ishtikhar ◽  
Gulam Rabbani ◽  
Shawez Khan ◽  
Rizwan Hasan Khan
Keyword(s):  
Thermal Stability ◽  
Antioxidant Activity ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Radical Scavenging Activity ◽  
Radical Scavenging ◽  
Interaction Mechanism ◽  
Scavenging Activity

Thymoquinone more strongly interacts with the ‘N’ isoform in comparison to the ‘B’ isoform of HSA and also increases its thermal stability but the antioxidant activity is significantly higher at the ‘B’ isoform of HSA.

scholarly journals A Comprehensive Study on the Biological Activity of Elderberry Extract and Cyanidin 3-O-Glucoside and Their Interactions with Membranes and Human Serum Albumin

Molecules ◽  
2018 ◽  
Vol 23 (10) ◽  
pp. 2566 ◽  
Author(s):  
Paulina Strugała ◽  
Sabrina Loi ◽  
Barbara Bażanów ◽  
Piotr Kuropka ◽  
Alicja Kucharska ◽  
...  
Keyword(s):  
Antioxidant Activity ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Breast Adenocarcinoma ◽  
Cyclooxygenase 1 ◽  
Mechanism Of Interaction ◽  
Liposomal Membranes ◽  
Lipid Aggregates ◽  
Static Mechanism

In our research we used the extract from dietary supplement of elderberry (EE) and its dominant anthocyanin—cyanidin 3-O-glucoside (Cy 3-gluc). By interacting with a model membrane that reflects the main lipid composition of tumor membranes, the extract components, including Cy 3-gluc, caused an increase in packing order, mainly in the hydrophilic region of the membrane. It can thus be stated that EE caused a rigidifying effect, which is fundamental for understanding its anticancer and antioxidant activity. This study represents the first attempt to unravel the mechanism of interaction of elderberry extract with membranes. The results of the interaction with human serum albumin (HSA) proved that the studied substance quenches the fluorescence of HSA through a static mechanism in which the main interaction forces are Van der Waals and hydrogen bonding. The antioxidant activity of EE and Cy 3-gluc on liposomal membranes, antiradical properties and ability to inhibited the activity of the enzymes cyclooxygenase-1 and cyclooxygenase-2 were also demonstrated. Moreover, the anticancer activity of EE and Cy 3-gluc on human breast adenocarcinoma cell line were investigated. In addition, EE also exhibited the ability to form lipid aggregates in the form of liposomal capsules that can be applied as carriers of active biological substances, and the highest efficacy of EE encapsulation was obtained for multilayered liposome formulations.

scholarly journals Quantitative evaluation of the role of cysteine and methionine residues in the antioxidant activity of human serum albumin using recombinant mutants

IUBMB Life ◽  
2012 ◽  
Vol 64 (5) ◽  
pp. 450-454 ◽  
Author(s):  
Yasunori Iwao ◽  
Yu Ishima ◽  
Junji Yamada ◽  
Taishi Noguchi ◽  
Ulrich Kragh-Hansen ◽  
...  
Keyword(s):  
Antioxidant Activity ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Quantitative Evaluation ◽  
Methionine Residues
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