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.
Department of Pharmaceutical Chemistry, School of Pharmacy, University of Pavia, Italy.
Stefania
S
Sabella
Milena
M
Quaglia
Cristina
C
Lanni
Marco
M
Racchi
Stefano
S
Govoni
Gabriele
G
Caccialanza
Alberto
A
Calligaro
Vittorio
V
Bellotti
Ersilia
E
De Lorenzi
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)