Exploring the Interaction Mechanism of Coumarin with Bovine β-Casein: Spectrofluorometric and Molecular Modeling Studies - Université Clermont Auvergne Accéder directement au contenu
Article Dans Une Revue Physical Chemistry Research Année : 2018

Exploring the Interaction Mechanism of Coumarin with Bovine β-Casein: Spectrofluorometric and Molecular Modeling Studies

Résumé

This paper is designed to examine the binding behavior of Coumarin with bovine -casein (βCN) through fluorescence spectroscopy and molecular modeling techniques. The data analysis on fluorescence titration experiments at various temperatures represents the enthalpy driven nature for the formation of Coumarin-βCN complex and the prevailed role of hydrogen bonds and van der Waals interactions in the binding process. The results also represent the static quenching of tryptophan and dynamics quenching of tyrosine and phenylalanine residues due to the binding of Coumarin. It can be concluded from molecular docking studies that Coumarin binds to several polar and nonpolar residues in the hydrophobic core of βCN with the binding energy of -6.96 kcal mol-1 . Finally, analysis of molecular dynamics (MD) simulation results suggested that the interactions between βCN and Coumarin are very stable and the binding of Coumarin restricted the flexibility of important residues in the binding site of this protein.
Fichier principal
Vignette du fichier
Exploring the Interaction Mechanism of Coumarin with Bovine β.pdf (580.37 Ko) Télécharger le fichier
Origine : Fichiers produits par l'(les) auteur(s)

Dates et versions

hal-04086050 , version 1 (01-05-2023)

Identifiants

Citer

Zahra Adibipour, Najmeh Fani, Abdol-Khalegh Bordbar, Mehdi Sahihi. Exploring the Interaction Mechanism of Coumarin with Bovine β-Casein: Spectrofluorometric and Molecular Modeling Studies. Physical Chemistry Research, 2018, 6 (3), pp.627-638. ⟨10.22036/pcr.2018.121289.1475⟩. ⟨hal-04086050⟩

Collections

PRES_CLERMONT
11 Consultations
22 Téléchargements

Altmetric

Partager

Gmail Facebook X LinkedIn More