Capillary electrophoresis studies on the aggregation process of beta-amyloid 1-42 and 1-40 peptides.
The possibility to monitor, in solution, the steps of beta-amyloid (Abeta) 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 Abeta 1-42 and Abeta 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.
Sabella
Stefania
S
Department of Pharmaceutical Chemistry, School of Pharmacy, University of Pavia, Italy.
Quaglia
Milena
M
Lanni
Cristina
C
Racchi
Marco
M
Govoni
Stefano
S
Caccialanza
Gabriele
G
Calligaro
Alberto
A
Bellotti
Vittorio
V
De Lorenzi
Ersilia
E
D016229:Amyloid beta-Peptides / Q000737:chemistry* / Q000648:ultrastructure; D019075:Electrophoresis, Capillary / Q000379:methods*; D008854:Microscopy, Electron; D010446:Peptide Fragments / Q000737:chemistry* / Q000648:ultrastructure; D014407:Tumor Cells, Cultured
D016229:Amyloid beta-Peptides; D010446:Peptide Fragments; C078592:amyloid beta-protein (1-40); C075222:amyloid beta-protein (1-42)