In Silico Study of the Interaction between Casein with Tocopherols: Preliminary Evaluation of Lipophilic Substrate Inclusion on Proteic Matrix

KNEETEMAN, MARÍA N.; GUNTERO, VANINA A.; FERRETTI, CRISTIÁN A.; GUTIERREZ, LEANDRO

Chemistry Proceedings

MDPI

Año: 2020 vol. 3

Bovine casein is a family of milk proteins with hydrophilic and hydrophobic regions thatshow block distribution within the protein chain. These amphiphilic properties offer great potentialas a material for use as a matrix for transporting active materials such as tocopherol. In this work,we aimed to evaluate the interaction of α1-casein, the main fraction of casein, with vitamin E bydocking calculations. Docking studies were conducted using SwissDock and DockThor servers.Using specific scoring functions based on energy terms, the best protein?ligand binding modelswere obtained. The observed interactions between vitamin E and amino acid residues consisted ofseveral hydrophobic interactions (e.g., with Tyr119, Ala144, Trp179, Met211, Pro212). A few hydrogen bonds were observed between the phenyl group of vitamin E and the carboxylate group ofthe glutamic acid residue (e.g., with Glu85, Glu148). In conclusion, the results suggest that there isa major interaction of vitamin E with random coil structure and interaction with segments formedby α-helix and β-sheet. This implies that in random coil segments there is a predominance of hydrophobic domains.