ArticleBiophysical journal2008
Hydration effects on the HET-s prion and amyloid-beta fibrillous aggregates, studied with three-dimensional molecular theory of solvation.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- How Water's Properties Are Encoded in Its Molecular Structure and Energies.Chemical reviews · 2017Article
- SAMPL5: 3D-RISM partition coefficient calculations with partial molar volume corrections and solute conformational sampling.Journal of computer-aided molecular design · 2016Article
- Small molecule hydration energy and entropy from 3D-RISM.Journal of physics. Condensed matter : an Institute of Physics journal · 2016Article
- Aβ(39-42) modulates Aβ oligomerization but not fibril formation.Biochemistry · 2012Article
- A peptide's perspective of water dynamics.Chemical physics · 2011Article
- Article
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4 authors.
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Abstract
We study the thermodynamic properties of the experimental fragments of the amyloid fibril made of the HET-s prion proteins (the infectious element of the filamentous fungus Podospora anserina) and of amyloid-beta proteins (the major component of Alzheimer's disease-associated plaques) by using the three-dimensional molecular theory of solvation. The full quantitative picture of hydration effects, including the hydration thermodynamics and hydration structure around the fragments, is presented. For both the complexes, the hydration entropic effects dominate, which results in the entropic part offsetting the unfavorable energetic part of the free energy change upon the association. This is in accord with the fact that the hydrophobic cooperativity plays an essential role in the formation of amyloid fibrils. By calculating the partial molar volume of the proteins, we found that the volume change upon the association in both the systems is large and positive, with the implication that high pressure causes destabilization of the fibril. This observation is in good agreement with the recent experimental results. We also found that both the HET-s and amyloid-beta pentamers have loose intermolecular packing with voids. The three-dimensional molecular theory of solvation predicts that water molecules can be locked in the interior cavities along the fibril axis for both the HET-s and amyloid-beta proteins. We provide a detailed molecular picture of the structural water localized in the interior of the fibrils. Our results suggest that the interior hydration plays an important role in the structural stability of fibrils.
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