Synthesis, Structure, and Physical Properties of a Barium Complex with 5-Sulfoisophthalic Acid Sodium Salt

2011 ◽  
Vol 637 (5) ◽  
pp. 596-601 ◽  
Author(s):  
Gang Wu ◽  
Fun-Jun Yin ◽  
Hao Wei ◽  
Zhen-Feng Liu ◽  
Xiao-Feng Wang
Keyword(s):  
Physical Properties ◽  
Sodium Salt ◽  
Acid Sodium Salt

The effect of the sweetness inhibitor 2(-4-methoxyphenoxy)propanoic acid (sodium salt) (Na-PMP) on the taste of bitter-sweet stimuli

1994 ◽  
Vol 19 (4) ◽  
pp. 349-358 ◽  
Author(s):  
Claire Johnson ◽  
Gordon G. Birch ◽  
Douglas B. MacDougall
Keyword(s):  
Sodium Salt ◽  
Propanoic Acid ◽  
Acid Sodium Salt

scholarly journals Ultrasound assisted green synthesis of bis(indol-3-yl)methanes catalyzed by 1-hexenesulphonic acid sodium salt

2010 ◽  
Vol 17 (2) ◽  
pp. 298-300 ◽  
Author(s):  
Ratnadeep S. Joshi ◽  
Priyanka G. Mandhane ◽  
Santosh D. Diwakar ◽  
Charansingh H. Gill
Keyword(s):  
Green Synthesis ◽  
Sodium Salt ◽  
Acid Sodium Salt ◽  
Ultrasound Assisted

Interaction between 2-(p-toluidino)-6-naphthalenesulfonic acid sodium salt (TNS) and β-lactoglobulin

2016 ◽  
Vol 94 (8) ◽  
pp. 680-686
Author(s):  
Huiqing Li ◽  
Jing Wei ◽  
Youming Dong ◽  
Zhiyue Yu
Keyword(s):  
Ligand Binding ◽  
Sodium Salt ◽  
Stable Complex ◽  
Sodium Dodecylbenzene Sulfonate ◽  
Ph Change ◽  
Hydrophobic Domain ◽  
Acid Sodium Salt ◽  
Wide Range ◽  
Β Lactoglobulin ◽  
Small Ligands

The major bovine milk protein β-lactoglobulin (β-LG), a member of the lipocalin superfamily, can bind a wide range of ligands and act as a transporter. In the present study, the combination of the hydrophobic molecule 2-(p-toluidino)-6-naphthalenesulfonic acid sodium salt (TNS) with β-LG was analyzed using fluorescence spectroscopy and AutoDock modeling to discern the major binding sites of the protein and to determine the capacity of other small ligands to bind with β-LG by utilizing TNS as a reference. The experimental data indicate that in a neutral pH environment, TNS is located in the hydrophobic domain of the protein, 2.5 nm away from the Trp19 residues of β-LG. The binding constant of the small molecule to β-LG is (3.30 ± 0.32) × 106 (mol L–1)−1. An interaction model between the ligand and β-LG was developed, and AutoDock modeling also demonstrates that the ligand is located in the central hydrophobic calyx of β-LG within the regions covered by the Förster radius of the Trp19–ligand pair. Although the interaction between the ligand and β-LG is affected by increasing ion strength, pH change, and heat treatment, the complex is maintained until the secondary structure of β-LG is destroyed. Additionally, the ligand binding stabilizes the folding of β-LG. The binding constants of sodium dodecyl sulfate (SDS) and sodium dodecylbenzene sulfonate (SDBS) to β-LG were obtained using competitive ligand binding measurements. With a sensitive fluorescence signal and stable complex, the ligand could be utilized as a reference to detect the binding of other small ligands to β-LG.

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