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Stabilization of protein structure by sugars

T Arakawa, S N Timasheff

    Biochemistry
    |December 7, 1982
    PubMed
    Summary

    Sugars like lactose and glucose preferentially interact with water, not proteins, leading to protein stabilization. This preferential hydration effect increases with protein surface area, influenced by sugar surface tension effects and exclusion volume.

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    Area of Science:

    • Biophysical Chemistry
    • Protein-Solvent Interactions
    • Solution Thermodynamics

    Background:

    • Proteins in aqueous solutions interact with solvent components.
    • Sugars are known to affect protein stability and behavior.
    • Understanding these interactions is crucial for protein formulation and function.

    Purpose of the Study:

    • To quantify the preferential interaction of proteins with solvent components in aqueous sugar solutions.
    • To elucidate the mechanisms behind sugar-induced protein stabilization and association.
    • To correlate preferential interaction with sugar properties like surface tension effects.

    Main Methods:

    • High-precision densimetry was employed to measure preferential interactions.
    • Aqueous solutions of proteins with lactose and glucose were analyzed.
    • Preferential interaction parameter was correlated with surface tension increments.

    Main Results:

    • Proteins were preferentially hydrated in both lactose and glucose solutions, indicating unfavorable free energy changes.
    • The degree of preferential hydration increased with increasing protein surface area.
    • A positive correlation was observed between preferential interaction and the sugars' surface tension increment.

    Conclusions:

    • Preferential hydration of proteins by water is a key mechanism for sugar-mediated stabilization.
    • Surface free energy perturbation by sugars plays a dominant role in their interaction with proteins.
    • Exclusion volume and protein surface chemistry also contribute to these interactions.

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