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

•Interaction of curcuminoids and BLG was studied using spectroscopic and computational methods.•The curcuminoids bind to the surface of BLG.•Results represent the conformational changes of BLG due its interaction with BDMC.

This study demonstrates the binding properties of bisdemethoxycurcumin (BDMC) and diacetylbisdemethoxycurcumin (DABC) as bioactive curcuminoids with bovine β-lactoglobulin (BLG) variant B using fluorescence and circular dichroism (CD) spectroscopy; molecular docking, and molecular dynamics simulation methods. The estimated binding constants for BLG-BDMC and BLG-DABC complexes were (8.99 ± 0.10) × 104 M−1 and (1.87 ± 0.10) × 102 M−1, respectively. The distances between BLG and these curcuminoids were obtained based on the Förster’s theory of non-radiative energy transfer. Molecular docking studies revealed the binding of BDMC and DABC to the protein surface cleft of protein by formation of four and one hydrogen bonds, respectively. Finally, molecular dynamics simulation results represent the conformational changes of BLG due to its interaction with BDMC. Also, the profiles of atomic fluctuations signified the rigidity of ligand binding site during the simulation.

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