title: Thermodynamic analysis of the aggregation propensity of oxidized Alzheimer's beta-amyloid variants.
abstract: 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.
authors.affiliation: Leibniz-Institut für Naturstoff-Forschung une Infektionsbiologie, Hans-Knöll-Institut, D-07745 Jena, Germany.
authors.forename: Peter
authors.initials: P
authors.lastname: Hortschansky
authors.forename: Tony
authors.initials: T
authors.lastname: Christopeit
authors.forename: Volker
authors.initials: V
authors.lastname: Schroeckh
authors.forename: Marcus
authors.initials: M
authors.lastname: Fändrich
mesh_terms: 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
chemical_list: D016229:Amyloid beta-Peptides; D010446:Peptide Fragments; C078592:amyloid beta-protein (1-40)