Comprehensive insights into the interaction mechanism between perfluorodecanoic acid and human serum albumin

2018 ◽  
Vol 42 (11) ◽  
pp. 9065-9073 ◽  
Author(s):  
Sichen Gao ◽  
Rutao Liu
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Interaction Mechanism ◽  
Toxic Effects ◽  
Interaction Mode ◽  
Perfluorodecanoic Acid ◽  
New Strategy

In this investigation, we explored the toxic effects of perfluorodecanoic acid (PFDA) on human serum albumin (HSA), established the interaction mode of PFDA with HSA, and provided a new strategy for the evaluation of toxicity of PFDA on functional proteins.

scholarly journals Interaction Mode of Dicumarol and Its Derivatives with Human Serum Albumin, .ALPHA.1-Acid Glycoprotein and Asialo .ALPHA.1-Acid Glycoprotein.

1992 ◽  
Vol 15 (1) ◽  
pp. 7-16 ◽  
Author(s):  
Mohammed Habibur RAHMAN ◽  
Toshimi MIYOSHI ◽  
Katsuaki SUKIMOTO ◽  
Akira TAKADATE ◽  
Masaki OTAGIRI
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Acid Glycoprotein ◽  
Interaction Mode

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 Investigation of the Interaction Mechanism between Salbutamol and Human Serum Albumin by Multispectroscopic and Molecular Docking

2020 ◽  
Vol 2020 ◽  
pp. 1-8
Author(s):  
Ting Zhao ◽  
Zihui Liu ◽  
Jingmei Niu ◽  
Baoxing Lv ◽  
Yuliang Xiao ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Fluorescence Spectra ◽  
Interaction Mechanism ◽  
Adrenergic Agonist ◽  
Airway Diseases ◽  
Synchronous Fluorescence Spectra ◽  
Multispectral Method

Salbutamol (SBAL), a kind of short-acting beta 2-adrenergic agonist, has been mainly used to treat bronchial asthma and other allergic airway diseases clinically. In this study, the interaction mechanism between salbutamol and human serum albumin was researched by the multispectral method and molecular docking. The fluorescence intensity of HSA could be regularly enhanced with the increase of SBAL concentration. Both the results of the multispectral method and molecular docking showed that SBAL could bind HSA with van der Waals force and hydrogen bonds. The binding mechanism was further analysed by UV-Vis and synchronous fluorescence spectra. The contents of the secondary structure of free HSA and SBAL-HSA complex were evaluated using CD spectra.

Synthesis of Three Cinnamamide Derivatives and Their Interaction Mechanism with Human Serum Albumin

2015 ◽  
Vol 36 (11) ◽  
pp. 1342-1352
Author(s):  
杜传荣 DU Chuan-rong ◽  
逯东伟 LU Dong-wei ◽  
石 康 SHI Kang ◽  
陈丹丹 CHEN Dan-dan ◽  
林翠梧 LIN Cui-wu
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Interaction Mechanism

Toxic effects of chrysoidine on human serum albumin: isothermal titration calorimetry and spectroscopic investigations

Luminescence ◽  
2015 ◽  
Vol 31 (2) ◽  
pp. 335-340 ◽  
Author(s):  
Haoyu Sun ◽  
Yingxue Liu ◽  
Meng Li ◽  
Songlin Han ◽  
Xudan Yang ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Isothermal Titration Calorimetry ◽  
Toxic Effects ◽  
Titration Calorimetry ◽  
Spectroscopic Investigations

scholarly journals Investigating the interaction mechanism of fluorescent whitening agents to human serum albumin using saturation transfer difference-NMR, multi-spectroscopy, and docking studies

RSC Advances ◽  
2017 ◽  
Vol 7 (44) ◽  
pp. 27796-27806 ◽  
Author(s):  
Ludan Zhao ◽  
Jiuyang Liu ◽  
Ronghui Guo ◽  
Qiaomei Sun ◽  
Hongqin Yang ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Interaction Mechanism ◽  
Docking Studies ◽  
Saturation Transfer ◽  
Saturation Transfer Difference ◽  
Fluorescent Whitening Agents ◽  
Std Nmr

Characterization of the interaction between two fluorescent whitening agents and human serum albumin: 1H STD-NMR, multi-spectroscopy, and docking studies.

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