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Thermodynamic analysis of the aggregation propensity of oxidized Alzheimer's β‐amyloid variants
Author(s) -
Hortschansky Peter,
Christopeit Tony,
Schroeckh Volker,
Fändrich Marcus
Publication year - 2005
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.051585905
Subject(s) - kinetics , chemistry , gibbs free energy , residue (chemistry) , peptide , protein aggregation , aggregate (composite) , amyloid (mycology) , biophysics , thermodynamics , biochemistry , biology , materials science , nanotechnology , physics , inorganic chemistry , quantum mechanics
We have determined the critical concentrations of a set of 18 variants of Alzheimer's Aβ(1–40) peptide, each carrying a different residue at position 18. We find that the critical concentrations depend on the hydrophobicity and β‐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 (ΔG), 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.