In silico study of the interaction between casein with tocopherols: preliminary evaluation of lipophilic substrate inclusion on proteic matrix.
Fecha
2020Autor
Guntero, Vanina A.
Gutierrez, Leandro
Kneeteman, María N.
Ferretti, Cristian A.
Metadatos
Mostrar el registro completo del ítemResumen
Bovine casein is a family of milk proteins with hydrophilic and hydrophobic regions that
show block distribution within the protein chain. These amphiphilic properties offer great potential as 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 by docking calculations. Docking studies were conducted by using SwissDock and DockThor servers. Using specific scoring functions based on energy terms were obtained the best protein-ligand binding models. The observed interactions between vitamin E and amino acid residues consisting of several hydrophobic interactions (e.g., with Tyr119, Ala144, Trp179, Met211, Pro212). A few hydrogen bonds were observed between phenyl group of vitamin E and carboxylate group of glutamic acid residue (e.g., with Glu85, Glu148). In conclusion, the results suggest that exists a major
interaction 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.
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