scholarly journals Open tubular columns containing the immobilized ligand binding domain of peroxisome proliferator-activated receptors α and γ for dual agonists characterization by frontal affinity chromatography with mass spectrometry detection

2013 ◽  
Vol 1284 ◽  
pp. 36-43 ◽  
Author(s):  
C. Temporini ◽  
G. Pochetti ◽  
G. Fracchiolla ◽  
L. Piemontese ◽  
R. Montanari ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Ligand Binding ◽  
Affinity Chromatography ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Peroxisome Proliferator ◽  
Mass Spectrometry Detection ◽  
Tubular Columns ◽  
Open Tubular Columns ◽  
Peroxisome Proliferator Activated Receptors

scholarly journals Docking of Phytochemicals to the Peroxisome Proliferator-Activated Receptor-Gamma Ligand Binding Domain

2012 ◽  
Vol 69 (2) ◽  
Author(s):  
Cristina COMAN ◽  
Carmen SOCACIU
Keyword(s):  
Hydrogen Bond ◽  
Ligand Binding ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Peroxisome Proliferator ◽  
Amino Acid Residues ◽  
Theoretical Level ◽  
Hydrogen Atoms ◽  
Peroxisome Proliferator Activated Receptor ◽  
Hydrogen Bond Interactions

In this study, the interaction between the phytochemical molecules - piperine and pipernonaline - and the ligand binding domain of the peroxisome proliferator-activated receptor-γ is investigated at a theoretical level by using the AutoDock software, which is a program that allows docking of molecular ligands to receptor macromolecules. The docking results show that the ligandreceptor complexes are formed through hydrogen bond interactions. The hydrogen bonds involve oxygen atoms in the piperine and pipernonaline ligands as hydrogen bond acceptors and hydrogen atoms from =NH or -NH groups of the amino acid residues in the receptor as hydrogen bond donors.  2

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