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.

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.

Biophysical insight into the interaction of levocabastine with human serum albumin: spectroscopy and molecular docking approach

2020 ◽  
pp. 1-10
Author(s):  
Fahad M. Almutairi ◽  
Mohammad Rehan Ajmal ◽  
Mohammad Khursheed Siddiqi ◽  
Nabeela Majid ◽  
Adel Ibrahim Ahmad Al-Alawy ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Docking Approach ◽  
Insight Into

In vitro studies on the interaction between human serum albumin and fosfomycin disodium salt, an antibiotic drug by multi-spectroscopic and molecular docking methods

2014 ◽  
Vol 41 (4) ◽  
pp. 2377-2387 ◽  
Author(s):  
Manjunath D. Meti ◽  
Kirthi S. Byadagi ◽  
Sharanappa T. Nandibewoor ◽  
Shrinivas D. Joshi ◽  
Uttam A. More ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Disodium Salt ◽  
In Vitro Studies ◽  
Antibiotic Drug
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