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Structural dynamics of the amyloid ?-protein monomer folding nucleus.


ABSTRACT: Alzheimer's disease (AD) is linked to the aberrant assembly of the amyloid ?-protein (A?). The (21)AEDVGSNKGA(30) segment, A?(21-30), forms a turn that acts as a monomer folding nucleus. Amino acid substitutions within this nucleus cause familial forms of AD. To determine the biophysical characteristics of the folding nucleus, we studied the biologically relevant acetyl-A?(21-30)-amide peptide using experimental techniques (limited proteolysis, thermal denaturation, urea denaturation followed by pulse proteolysis, and electron microscopy) and computational methods (molecular dynamics). Our results reveal a highly stable foldon and suggest new strategies for therapeutic drug development.

SUBMITTER: Roychaudhuri R 

PROVIDER: S-EPMC3362201 | biostudies-literature | 2012 May

REPOSITORIES: biostudies-literature

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Structural dynamics of the amyloid β-protein monomer folding nucleus.

Roychaudhuri Robin R   Yang Mingfeng M   Condron Margaret M MM   Teplow David B DB  

Biochemistry 20120507 19


Alzheimer's disease (AD) is linked to the aberrant assembly of the amyloid β-protein (Aβ). The (21)AEDVGSNKGA(30) segment, Aβ(21-30), forms a turn that acts as a monomer folding nucleus. Amino acid substitutions within this nucleus cause familial forms of AD. To determine the biophysical characteristics of the folding nucleus, we studied the biologically relevant acetyl-Aβ(21-30)-amide peptide using experimental techniques (limited proteolysis, thermal denaturation, urea denaturation followed by  ...[more]

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