Thermal expansivity of amyloid β16–22peptides and their aggregates in water
Literature Information
I. Brovchenko, R. R. Burri, A. Krukau, A. Oleinikova
Temperature dependence of the volumetric and structural properties of Aβ16–22 peptides (wild type and pathogenic forms) and their aggregates in water was studied by simulations. The intrinsic thermal expansion coefficient αp of peptides was evaluated by taking into account the difference between the volumetric properties of hydration and bulk water. Single peptides show mainly positive values of αp that correlates with the increasing number of intrapeptide hydrogen bonds upon heating. Negative values of αp found for large peptide aggregates may be attributed to the shrinking of voids inside aggregates with increasing temperature or to their rubber-like elasticity. The peptide surface exposed to water becomes more hydrophobic with increasing aggregate size that appears in decreasing density of hydration water and evidences a hydrophilic character of aggregation.
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