Protein Regge Trajectories, Phase Coexistence and Physics of Alzheimer's Disease

Bibliographic Details
Title: Protein Regge Trajectories, Phase Coexistence and Physics of Alzheimer's Disease
Authors: Krokhotin, Andrei, Niemi, Antti J.
Publication Year: 2011
Collection: Condensed Matter
Physics (Other)
Quantitative Biology
Subject Terms: Quantitative Biology - Biomolecules, Condensed Matter - Soft Condensed Matter, Physics - Biological Physics
More Details: Alzheimer's disease causes severe neurodegeneration in the brain that leads to a certain death. The defining factor is the formation of extracellular senile amyloid plaques in the brain. However, therapeutic approaches to remove them have not been effective in humans, and so our understanding of the cause of Alzheimer's disease remains incomplete. Here we investigate physical processes that might relate to its onset. Instead of the extracellular amyloid, we scrutinize the intracellular domain of its precursor protein. We argue for a phenomenon that has never before been discussed in the context of polymer physics: Like ice and water together, the intracellular domain of the amyloid precursor protein forms a state of phase coexistence with another protein. This leads to an inherent instability that could well be among the missing pieces in the puzzle of Alzheimer's disease.
Comment: 4 figures
Document Type: Working Paper
Access URL: http://arxiv.org/abs/1109.1221
Accession Number: edsarx.1109.1221
Database: arXiv
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  Data: Condensed Matter<br />Physics (Other)<br />Quantitative Biology
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  Data: Alzheimer's disease causes severe neurodegeneration in the brain that leads to a certain death. The defining factor is the formation of extracellular senile amyloid plaques in the brain. However, therapeutic approaches to remove them have not been effective in humans, and so our understanding of the cause of Alzheimer's disease remains incomplete. Here we investigate physical processes that might relate to its onset. Instead of the extracellular amyloid, we scrutinize the intracellular domain of its precursor protein. We argue for a phenomenon that has never before been discussed in the context of polymer physics: Like ice and water together, the intracellular domain of the amyloid precursor protein forms a state of phase coexistence with another protein. This leads to an inherent instability that could well be among the missing pieces in the puzzle of Alzheimer's disease.<br />Comment: 4 figures
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      – SubjectFull: Quantitative Biology - Biomolecules
        Type: general
      – SubjectFull: Condensed Matter - Soft Condensed Matter
        Type: general
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      – TitleFull: Protein Regge Trajectories, Phase Coexistence and Physics of Alzheimer's Disease
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