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Context dependence of protein misfolding and structural strains in neurodegenerative diseases
Author(s) -
Mehta Anil K.,
Rosen Rebecca F.,
Childers W. Seth,
Gehman John D.,
Walker Lary C.,
Lynn David G.
Publication year - 2013
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.22283
Subject(s) - chemistry , context (archaeology) , computational biology , amyloid (mycology) , identification (biology) , pittsburgh compound b , protein folding , amyloid fibril , disease , neuroscience , amyloid β , biochemistry , alzheimer's disease , biology , paleontology , medicine , inorganic chemistry , botany , pathology
Vast arrays of structural forms are accessible to simple amyloid peptides and environmental conditions can direct assembly into single phases. These insights are now being applied to the aggregation of the Aβ peptide of Alzheimer's disease and the identification of causative phases. We extend use of the imaging agent Pittsburgh compound B to discriminate among Aβ phases and begin to define conditions of relevance to the disease state. Also, we specifically highlight the development of methods for defining the structures of these more complex phases. © 2013 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 100: 722–730, 2013.