High Pressure Modulates Amyloid Formation

Title: High Pressure Modulates Amyloid Formation

Volume: 13 Issue: 3

Author(s): Joan Torrent, Claude Balny and Reinhard Lange

Affiliation:

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

Abstract: 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.

Cite this article as:

Torrent Joan, Balny Claude and Lange Reinhard, High Pressure Modulates Amyloid Formation, Protein & Peptide Letters 2006; 13 (3) . https://dx.doi.org/10.2174/092986606775338371

DOI https://dx.doi.org/10.2174/092986606775338371	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305