Thermodynamic analysis of the aggregation propensity of oxidized Alzheimer's beta-amyloid variants.
We have determined the critical concentrations of a set of 18 variants of Alzheimer's Abeta(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 (DeltaG), 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.
Hortschansky
Peter
P
Leibniz-Institut für Naturstoff-Forschung une Infektionsbiologie, Hans-Knöll-Institut, D-07745 Jena, Germany.
Christopeit
Tony
T
Schroeckh
Volker
V
Fändrich
Marcus
M
D016229:Amyloid beta-Peptides / Q000737:chemistry*; D057927:Hydrophobic and Hydrophilic Interactions; D007700:Kinetics; D010084:Oxidation-Reduction; D010446:Peptide Fragments / Q000737:chemistry*; D017433:Protein Structure, Secondary; D012995:Solubility; D013816:Thermodynamics
D016229:Amyloid beta-Peptides; D010446:Peptide Fragments; C078592:amyloid beta-protein (1-40)