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Amyloidogenic Protein–Membrane Interactions: Mechanistic Insight from Model Systems
Author(s) -
Butterfield Sara M.,
Lashuel Hilal A.
Publication year - 2010
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200906670
Subject(s) - membrane , amyloid (mycology) , biophysics , chemistry , membrane protein , cell membrane , microbiology and biotechnology , peptide , biochemistry , biology , inorganic chemistry
Abstract The toxicity of amyloid‐forming proteins is correlated with their interactions with cell membranes. Binding events between amyloidogenic proteins and membranes result in mutally disruptive structural perturbations, which are associated with toxicity. Membrane surfaces promote the conversion of amyloid‐forming proteins into toxic aggregates, and amyloidogenic proteins, in turn, compromise the structural integrity of the cell membrane. Recent studies with artificial model membranes have highlighted the striking resemblance of the mechanisms of membrane permeabilization of amyloid‐forming proteins to those of pore‐forming toxins and antimicrobial peptides.