Understanding the mode of binding mechanism of doripenem to human serum albumin: Spectroscopic and molecular docking approaches

2018 ◽  
Vol 31 (7) ◽  
pp. e2710 ◽  
Author(s):  
Lubna Maryam ◽  
Ashima Sharma ◽  
Mohd W. Azam ◽  
Shahper N. Khan ◽  
Asad U. Khan
Keyword(s):  
Molecular Docking ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Mechanism

scholarly journals Probing the interaction mechanism between Direct Red 80 and Human serum albumin: studies at the molecular level

2021 ◽  
Vol 245 ◽  
pp. 03060
Author(s):  
Yan Song ◽  
Yuzhi Shi ◽  
Kejia Zhang
Keyword(s):  
Molecular Docking ◽  
Secondary Structure ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Molecular Level ◽  
Interaction Mechanism ◽  
Consumer Health ◽  
Binding Mechanism ◽  
Endogenous Fluorescence

In recent years, azo dyes have received increasing attention due to their adverse effects on the environment and consumer health. However, the interaction mechanism between human serum albumin (HSA) and Direct Red 80 (DR80) is still unknown. The results showed that DR80 changed the secondary structure of HSA and made HSA skeleton loose and stretch. In addition, DR80 quenched the endogenous fluorescence of HSA by static quenching and changed the microenvironment of Trp in form of the hydrophobicity increased and the polarity decreased. Molecular docking results indicated that DR80 bound to the interface of three α-helical domains of HSA, hence, the changes in HSA structure and conformation was the main reason for the decline of its esterase activity. This work was done to illuminate the binding mechanism of DR80 and HSA, and to provide a different way for screening the low toxic dye at the molecular level.

Binding mechanism of tauroursodeoxycholic acid to human serum albumin: insights from NMR relaxation and docking simulations

RSC Advances ◽  
2015 ◽  
Vol 5 (15) ◽  
pp. 11036-11042 ◽  
Author(s):  
Di Wu ◽  
Yuanming Zhai ◽  
Jin Yan ◽  
Kailin Xu ◽  
Qing Wang ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Nmr Relaxation ◽  
Binding Mechanism ◽  
Tauroursodeoxycholic Acid ◽  
Docking Simulations ◽  
Relationship Of

Binding patterns and structure–affinity relationship of tauroursodeoxycholic acid with human serum albumin were established by NMR methodology and docking simulations.

Chromatographic Framework to Determine the Memantine Binding Mechanism on Human Serum Albumin Surface

2008 ◽  
Vol 68 (3-4) ◽  
pp. 179-186 ◽  
Author(s):  
Firas Ibrahim ◽  
Yves-Claude Guillaume ◽  
Claire André
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Mechanism
Sign in / Sign up

Export Citation Format

Share Document