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Published online before print June 2, 2006, 10.1110/ps.062116206
Protein Science (2006), 15:1801-1805. Published by Cold Spring Harbor Laboratory Press. Copyright © 2006 The Protein Society
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FOR THE RECORD

Mutagenic exploration of the cross-seeding and fibrillation propensity of Alzheimer's beta-amyloid peptide variants

Alexander Peim1, Peter Hortschansky2, Tony Christopeit1, Volker Schroeckh2, Walter Richter3 and Marcus Fändrich1

1 Leibniz-Institut für Altersforschung, D-07745 Jena, Germany
2 Leibniz-Institut für Naturstoff-Forschung und Infektionsbiologie, D-07745 Jena, Germany
3 Elektronenmikroskopisches Zentrum am Klinikum der Friedrich-Schiller-Universität Jena, D-07743 Jena, Germany

(RECEIVED January 26, 2006; FINAL REVISION March 15, 2006; ACCEPTED March 26, 2006)

Amyloid formation is a nucleation-dependent process that is accelerated dramatically in vivo and in vitro upon addition of appropriate fibril seeds. A potent species barrier can be effective in this reaction if donor and recipient come from different biological species. This species barrier is thought to reflect differences in the amino acid sequence between seed and target polypeptide. Here we present an in vitro mutagenic cross-seeding analysis of Alzheimer's Abeta(1-40) peptide in which we mapped out the effect of systematically varied amino acid replacements on the propensity of seed-dependent amyloid fibril formation. We find that the susceptibility of different peptides toward cross-seeding relates to the intrinsic aggregation propensity of the respective polypeptide chain and, therefore, to properties such as beta-sheet propensity and hydrophobicity. These data imply that the seed-dependent formation of amyloid-like fibrils is affected by the intrinsic properties of the polypeptide chain in a manner that is similar to what has been described previously for aggregation reactions in general. Hence, the nucleus acts in this case as a catalyst that promotes the fibrillation of different polypeptide chains according to their intrinsic structural predilection.

Keywords: amyloid; conformational disease; neurodegeneration; protein folding; prion


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J. Meinhardt, G. G. Tartaglia, A. Pawar, T. Christopeit, P. Hortschansky, V. Schroeckh, C. M. Dobson, M. Vendruscolo, and M. Fandrich
Similarities in the thermodynamics and kinetics of aggregation of disease-related Abeta(1-40) peptides
Protein Sci., June 1, 2007; 16(6): 1214 - 1222.
[Abstract] [Full Text] [PDF]


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