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

V. GUNTERO; L. GUTIERREZ; M. KNEETEMAN; C. FERRETTI

Santiago de Compostela

Conferencia; The 24th International Electronic Conference on Synthetic Organic Chemistry; 2020

Universidad de Santiago de Compostela

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 being used as a matrix for transport active materials as tocopherol. In this work,we aim to evaluate the interaction of α1-casein, the main fraction of the casein, with vitamin E bydocking calculations. Docking studies were conducted by using SwissDock and DockThor servers.Using specific scoring functions based on energy terms were obtained the best protein-ligandbinding models. The observed interactions between vitamin E and amino acid residues consistingof several hydrophobic interactions (e.g., with Tyr119, Ala144, Trp179, Met211, Pro212). A fewhydrogen bonds were observed between phenyl group of vitamin E and carboxylate group ofglutamic acid residue (e.g., with Glu85, Glu148). In conclusion, the results suggest that exists a majorinteraction of vitamin E with random coil structure that the interaction with segments formed by α-helix and β-sheet. This implies that in random coil segments predominance hydrophobic domains.