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Finding harmless stabilizing compounds for proteins and nucleic acids is an important task in modern food and pharmaceutical industries. In this work sucrose and trehalose were investigated as stabilizing agents for myoglobin and the Aβ(1-42) peptide. Atomistic molecular dynamics (MD) simulations were carried out for several systems of myoglobin/Aβ(1-42) in both water and aqueous solutions of sucrose or trehalose. Analysis of resulting MD trajectories and computed self-intermediate scattering functions showed that trehalose slowed down the dynamics of myoglobin and Aβ(1-42) more than sucrose. The difference was particularly large in the case of Aβ(1-42). It was also observed that the rotational motions of the disaccharide molecules slowed down by the presence of myoglobin/Aβ(1-42), and also in this case the effect was largest for Aβ(1-42). Perhaps slightly unexpected from the observed dynamics, it was found that the trehalose molecules exhibited less direct interactions with myoglobin/Aβ(1-42) than sucrose, but caused a stronger reduction of the water dynamics in the hydration shell of myoglobin/Aβ(1-42), and thereby also slowed down and stabilized myoglobin/Aβ(1-42) more efficiently. This mechanism can explain why trehalose generally is a better stabilizing agent than sucrose and other types of sugar.
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