Spectroscopic and molecular modeling probing of biophysical influence of β-casein nano-protein on adrenaline and arachidonoyl adrenaline
Résumé
The interaction mechanism of adrenaline and arachidonoyl adrenalin with β-casein milk protein as a nano-carrier was investigated by fluorescence spectroscopy, molecular docking, and molecular dynamics simulation approaches. The results of fluorescence studies and thermodynamic parameters revealed the negative values of enthalpy and entropy changes for both compounds which illustrate the vital role of hydrogen bond and van der Waals interaction in stabilizing protein-ligand complexes. The docking studies showed that adrenaline binds to several polar and non-polar residues in the inner hydrophobic core of β-casein with binding energy of − 27.25 kJ mol −1 but arachidonoyl adrenalin binds in a core near the surface of this protein with the binding energy of − 28.67 kJ mol −1. Finally, the molecular dynamics simulation results suggested that the interactions between protein and both compounds are very stable and during the whole simulation time no significant protein structure changes were observed, consequently βcasein can be considered as a suitable carrier for adrenaline and arachidonoyl adrenalin.
Domaines
Chimie théorique et/ou physique
Fichier principal
Spectroscopic and molecular modeling probing of biophysical influence of β.pdf (1008.54 Ko)
Télécharger le fichier
Origine : Fichiers produits par l'(les) auteur(s)