High Pressure Modulates Amyloid Formation

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A common mechanism of conformational changes and pathological aggregation of proteins associated with amyloid diseases remains to be proven. High pressure is emerging as a new strategy for studying aspects of amyloid formation. Pressure provides a convenient means to populate and characterize partially folded states, which are thought to have a key role in assembly processes of proteins into amyloid fibrils. High pressure can also be used to dissociate aggregates and amyloid fibrils or on the opposite to generate such species.

Keywords: Amyloid; fibrils; high pressure; prion; protein aggregation; protein conformation; protein folding

Document Type: Research Article

DOI: http://dx.doi.org/10.2174/092986606775338371

Affiliations: INSERM U710, CC 105, Universite Montpellier 2, Place Eugene Bataillon, F-34095 Montpellier cédex 5, France.

Publication date: March 1, 2006

More about this publication?
  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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