NDLI: Beta-barrel models of soluble amyloid beta oligomers and annular protofibrils.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Shafrir, Yinon Durell, Stewart R. Anishkin, Andriy Guy, H. Robert
Description	Country affiliation: United States Author Affiliation: Shafrir Y ( Laboratory of Cell Biology, CCR, NCI, National Institutes of Health, Bethesda, Maryland, USA.)
Abstract	Both soluble and membrane-bound prefibrillar assemblies of Abeta (Aß) peptides have been associated with Alzheimer's disease (AD). The size and nature of these assemblies vary greatly and are affected by many factors. Here, we present models of soluble hexameric assemblies of Aß42 and suggest how they can lead to larger assemblies and eventually to fibrils. The common element in most of these assemblies is a six-stranded ß-barrel formed by the last third of Aß42, which is composed of hydrophobic residues and glycines. The hydrophobic core ß-barrels of the hexameric models are shielded from water by the N-terminus and central segments. These more hydrophilic segments were modeled to have either predominantly ß or predominantly secondary structure. Molecular dynamics simulations were performed to analyze stabilities of the models. The hexameric models were used as starting points from which larger soluble assemblies of 12 and 36 subunits were modeled. These models were developed to be consistent with numerous experimental results.
File Format	HTM / HTML
ISSN	08873585
e-ISSN	10970134
DOI	10.1002/prot.22832
Journal	Proteins: Structure, Function, and Bioinformatics
Issue Number	16
Volume Number	78
Language	English
Publisher	Wiley-Liss
Publisher Date	2010-12-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Research Support, N.i.h., Extramural Amino Acid Sequence Cell Membrane Protein Structure, Secondary Solubility Discipline Biochemistry Amyloid Beta-peptides Models, Molecular Molecular Sequence Data Research Support, N.i.h., Intramural Molecular Dynamics Simulation Chemistry Protein Structure, Quaternary
Content Type	Text
Resource Type	Article
Subject	Structural Biology Biochemistry Molecular Biology

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