Dynamic Aspects of Amyloid Fibrils of α-Synuclein Related to the Pathogenesis of Parkinson’s Disease

Fujiwara, Satoru

doi:10.4172/2161-0460.1000310

Cited by 1 publication

(2 citation statements)

References 38 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Large solvent-filled space within the fibrils is required to this. αS fibrils are disordered except for the core structure [22,55]. In agreement with this fact, we found that the amyloid form of αS can be considered as disordered to 75(3)% regarding the nature of its SAS.…”

Section: Discussionsupporting

confidence: 82%

“…We suggest that this can be the cause of the low level of mobile hydration for αS amyloids. The potential barrier distribution affecting the motion of mobile hydration water is mainly heterogeneous in the αS amyloids, due to the abundant solvent-exposed side chains, the motion of which have bigger amplitudes than in the αS monomers [22,55]. Large solvent-filled space within the fibrils is required to this.…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

WT and A53T α-Synuclein Systems: Melting Diagram and Its New Interpretation

Bokor

Tantos

Tompa

et al. 2020

IJMS

View full text Add to dashboard Cite

The potential barriers governing the motions of α-synuclein (αS) variants’ hydration water, especially energetics of them, is in the focus of the work. The thermodynamical approach yielded essential information about distributions and heights of the potential barriers. The proteins’ structural disorder was measured by ratios of heterogeneous water-binding interfaces. They showed the αS monomers, oligomers and amyloids to possess secondary structural elements, although monomers are intrinsically disordered. Despite their disordered nature, monomers have 33% secondary structure, and therefore they are more compact than a random coil. At the lowest potential barriers with mobile hydration water, monomers are already functional, a monolayer of mobile hydration water is surrounding them. Monomers realize all possible hydrogen bonds with the solvent water. αS oligomers and amyloids have half of the mobile hydration water amount than monomers because aggregation involves less mobile hydration. The solvent-accessible surface of the oligomers is ordered or homogenous in its interactions with water to 66%. As a contrast, αS amyloids are disordered or heterogeneous to 75% of their solvent accessible surface and both wild type and A53T amyloids show identical, low-level hydration. Mobile water molecules in the first hydration shell of amyloids are the weakest bound compared to other forms.

show abstract

Section: Discussionsupporting

confidence: 82%

Section: Discussionmentioning

confidence: 99%