NDLI: The aggregation kinetics of Alzheimer's beta-amyloid peptide is controlled by stochastic nucleation.

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The aggregation kinetics of Alzheimer's beta-amyloid peptide is controlled by stochastic nucleation.

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The aggregation kinetics of Alzheimer's beta-amyloid peptide is controlled by stochastic nucleation.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Zandomeneghi, Giorgia Hortschansky, Peter Christopeit, Tony Schroeckh, Volker Fändrich, Marcus
Description	Country affiliation: Germany Author Affiliation: Hortschansky P ( Institut für Molekulare Biotechnologie (IMB), Jena, Germany.)
Abstract	We report here a recombinant expression system that allows production of large quantities of Alzheimer's Abeta(1-40) peptide. The material is competent to dissolve in water solutions with 'random-coil properties,' although its conformation and factual oligomerization state are determined by the physico-chemical solution conditions. When dissolved in 50 mM sodium phosphate buffer (pH 7.4) at 37 degrees C, the peptide is able to undergo a nucleated polymerization reaction. The aggregation profile is characteristically bipartite, consisting of lag and growth phase. From these curves we determined the lag time as well as the rate of aggregation. Both values were found to depend on peptide concentration and addition or formation of seeds. Moreover, they can vary considerably between apparently identical samples. These data imply that the nucleation event is under influence of a stochastic factor that can manifest itself in profound macroscopic differences in the aggregation kinetics of otherwise indistinguishable samples.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	7
Volume Number	14
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2005-07-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Amyloid Beta-peptides Chemistry Metabolism Peptide Fragments Protein Folding Genetics Isolation & Purification Circular Dichroism Computer Simulation Endopeptidases Histidine Kinetics Mutation Protein Conformation Solubility Spectroscopy, Fourier Transform Infrared Thiazoles Comparative Study Research Support, Non-u.s. Gov't Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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