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Published online before print September 30, 2005, 10.1110/ps.051585905
Protein Science (2005), 14:2915-2918. Published by Cold Spring Harbor Laboratory Press. Copyright © 2005 The Protein Society
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FOR THE RECORD

Thermodynamic analysis of the aggregation propensity of oxidized Alzheimer’s {beta}-amyloid variants

Peter Hortschansky1, Tony Christopeit2, Volker Schroeckh1 and Marcus Fändrich2

1 Leibniz-Institut für Naturstoff-Forschung und Infektionsbiologie, Hans-Knöll-Institut, D-07745 Jena, Germany
2 Institut für Molekulare Biotechnologie (IMB), D-07745 Jena, Germany

(RECEIVED May 12, 2005; FINAL REVISION July 8, 2005; ACCEPTED August 5, 2005)

We have determined the critical concentrations of a set of 18 variants of Alzheimer’s A{beta}(1–40) peptide, each carrying a different residue at position 18. We find that the critical concentrations depend on the hydrophobicity and {beta}-sheet propensity of residue 18, and therefore on properties that we identified previously to affect also the kinetics by which these peptides aggregate. Since the critical concentrations can be related to the Gibbs free energy of aggregation ({Delta}G), these data imply a link between the thermodynamics and the kinetics of aggregation in that sequences that form very stable aggregates are also those that form such aggregates very rapidly.

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

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.051585905.

Reprint requests to: Marcus Fändrich, Institut für Molekulare Biotechnologie (IMB), Beutenbergstraße 11, D-07745 Jena, Germany; e-mail: fandrich{at}imb-jena.de; fax: +49-3641-656310.


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