Spectrofluoremetric and molecular docking study on the interaction of bisdemethoxycurcumin with bovine β-casein nanoparticles

Multispectroscopic and molecular modeling studies on the interaction of two curcuminoids with β-lactoglobulin

“…This inadequacy could be removed by loading of these bioactive compounds in carrier proteins. In our previous studies, the ability of serum albumins and beta-casein for transporting of these bioactive compounds were investigated by exploring the binding mechanism [29], [30], [31]. In the present study, the interaction of BDMC and DABC with BLG have been comprehensively investigated by using various spectroscopic and molecular modeling methods in order to explore the binding properties of these systems and evaluating the capability of BLG to transport these curcuminoids.…”

Bovine β‐casein binding studies of a Schiff base ligand: fluorescence and circular dichroism approaches

“…Next, solutions were dialyzed against phosphate buffer for 24 h at 4°C, to prevent formation of Ca 2 + bridges using 1 mM EDTA solution. [ 18 ] After dialysis, the β‐CN concentration was specified spectrophotometrically as ε = 0.44 ml mg −1 cm −1 at 280 nm. [ 19 ]…”

A combination of spectroscopic and molecular docking techniques to study interaction of bis(indolyl)methane with bovine milk α-casein

“…Docking experiments were carried out to visualize the binding site of BIM to α-casein. All the docking calculations were performed using Autodock 4.2 Tools [33,34] . The macromolecule was kept rigid, while all the torsional bonds of ligands were set free to rotate.…”

“…Eqs. (7)-(9) made it possible to calculate that R o ¼ 3:30 nm, r ¼ 2:78 nm, J ¼ 8:11 Â 10 À15 cm 3 mol À1 L. The distance between the donor and acceptor ðrÞ is less than 7 nm, indicating that the mechanism of energy transfer for quenching is non-radiative [33,34] . The short distance values suggested a strong interaction between BIM and tryptophan residues in β-casein.…”