In-silico study of vitamin E complexation with Bubalus bubalis whey

LEANDRO FABIÁN BUSTOS; FRANCO EMANUEL VASILE; JUDIS MARÍA ALICIA; OSCAR EDGARDO PEREZ

Conferencia; 1st Zooming into Preclinical Nanomedicines in the era of COVID-19; 2020

Asociación Argentina de Nanomedicinas - Nanomed Ar

The complexation of α-tocopherol (the most active form of vitamin E) with buffalo whey proteins constitutes a novel strategy for its protection and vehiculization in drugs or foods. Increasing the stability of this bioactive compound against environmental factors as light, oxygen and heat, could contribute to guarantee its final disposal and preventing Vitamin E deficiency diseases. Thus, the objective of this work was to study the interaction of dl-α-tocopherol acetate (α-toc) with the main whey proteins of Bubalus bubalis: α-lactalbumin (α-lac), β-lactoglobulin (β-lg) and bovine serum albumin (BSA), through of molecular docking. With this purpose, a α-toc conformer was docked against the crystal structures of α-lac, β-lg and BSA using Autodock Vina. The α-toc binding modes with lowest energy corresponded to its assembly in the cleft region of the α-lac, inside the β-barrel of the β-lg, and in a pocket placed at the interface of subdomains I and III of the BSA. The binding energies and number interactions were -5.5 (10), -7.5 (16) and -7.4 (14) kcal/mol, respectively. These results contribute to characterize the interactions of the α-toc with the main individual whey proteins of Bubalus bubalis, which will allow to optimize the encapsulation of this vitamin using a buffalo whey protein concentrate.