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oa Editorial [Hot topic: Membrane Interactions of Amyloid Proteins and Peptides (Guest Editor: Raz Jelinek)]
- Source: Current Protein and Peptide Science, Volume 11, Issue 5, Aug 2010, p. 318 - 318
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- 01 Aug 2010
Abstract
The growing interest in membrane interactions of amyloidogenic peptides and proteins emanates from the realization that lipids and membranes play important, potentially central, roles in the toxicity and pathological pathways of amyloid diseases. Expanding body of evidence indicates that lipid binding of amyloidogenic peptides, and amyloid peptide association with cellular membranes are critical to the onset and progression of amyloid diseases. Conversely, membranes and membrane components appear to intimately affect the aggregation properties, and consequently the biological functions, of varied amyloidogenic proteins. This special issue of CPPS aims to provide an overview of important aspects on the cutting edge of this field. This Issue encompasses contributions from leading researchers, focusing on central phenomena involving aspects pertaining to lipid- and membrane-interactions of amyloidogenic peptides and proteins. Eckert et al. summarize the large body of experimental evidence pertaining to amyloid-β interactions with lipid bilayers and specific components within the bilayers. Henriques and Castanho focus on the prion system, and discuss the molecular interactions and biological significance of membrane interactions of an amyloidogenic fragment of the prion protein (PrP). Van Rooijen et al. concentrate upon membrane interactions of α-synuclein, in particular the roles of oligomeric species of the protein in induction of toxicity. Stefani expanded on the issue of amyloid oligomers, and provides a comprehensive overview on amyloid polymorphism and the relationship between this often-encountered phenomenon and membrane interactions and cell toxicity. Otzen presents a biophysical analysis of amyloid peptide structural studies carried out in model membrane systems, while Jelinek and Sheynis highlight the occasionally conflicting conclusions drawn from studies using different membrane models and experimental techniques.