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Capillary electrophoresis studies on the aggregation process of β‐amyloid 1‐42 and 1‐40 peptides
Author(s) -
Sabella Stefania,
Quaglia Milena,
Lanni Cristina,
Racchi Marco,
Govoni Stefano,
Caccialanza Gabriele,
Calligaro Alberto,
Bellotti Vittorio,
De Lorenzi Ersilia
Publication year - 2004
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.200406062
Subject(s) - capillary electrophoresis , chemistry , electrophoresis , ultracentrifuge , oligomer , analytical ultracentrifugation , nucleation , amyloid (mycology) , protein aggregation , small molecule , biophysics , chromatography , biochemistry , biology , organic chemistry , inorganic chemistry
The possibility to monitor, in solution, the steps of β‐amyloid (Aβ) nucleation and therefore to describe this dynamic process by using capillary electrophoresis and under optimized experimental conditions is described. Striking differences in the electrophoretic patterns of Aβ 1‐42 and Aβ 1‐40 over time are here shown, and different aggregation states are elucidated, which reflect the very diverse oligomerization behavior of two very similar peptides. The isolation of one aggregated species of high molecular weight by ultracentrifugation allowed us to assess its role as toxic oligomer. The perturbation of the existing equilibrium among the identified species by the addition of small molecules can in principle interfere with the aggregation process of the peptides and ultimately prevent the plaque formation in vitro .