Visualizing structural changes of egg avidin to thermal and electric field stresses by molecular dynamics simulation

Abstract

Eggs are one of the most common ingredients used by human beings due to their nutritional attributes and health benefits. However, eggs also contain an anti-nutrient known as avidin, which forms an avidin-biotin complex, resulting in biotin unavailable in the body for absorption. In the present study, molecular dynamics (MD) simulation was used to evaluate the effect of external stresses, including thermal and oscillating electric field (0.05 V/nm, 2450 MHz) at 300–353 K on the structural properties of avidin. The modeling was performed using a GROningen MAchine for Chemical Simulations (GROMACS) software. The alteration in conformation of avidin was evaluated in terms of the number of hydrogen bonds, root mean square deviation, the radius of gyration, and solvent accessible surface area. The application of thermal stress and electric field resulted in conformational changes in the avidin protein. The results also showed that hydrogen bonds have a significant influence on the stability of alpha-helices, which are responsible for the compactness of the molecule. Change in the hydrogen bonds can increase the surface area and hence the surface properties of avidin significantly. Thermal combined with electric field showed an application in inhibiting the activity of avidin present in egg white.