Conformational Changes of the Amyloidβ-Peptide (1-40) Adsorbed on Solid Surfaces

摘要: The conformational change of the 39-43 residues amyloid beta-peptide (Abeta) toward a beta-sheet enriched state promotes self-aggregation peptide molecules and constitutes major component plaques in Alzheimer patients. crucial question behind Abeta is related to different pathways may take after cleavage from precursor proteins at cellular membranes. This work aiming determining conformation (1-40) adsorbed on hydrophobic Teflon hydrophilic silica particles, as model sorbent surfaces mimicking apolar transmembrane environment polar, charged membrane surface, respectively. mechanism by which interacts with solid strongly depends hydrophobic/hydrophilic character particles. Hydrophobic electrostatic interactions contribute differently each case, causing completely two surfaces. When between prevail, mainly adopts an alpha-helix due H-bonding part that oriented towards surface. On other hand, when adsorbs formation promoted intermolecular association parts peptide. Irrespective characteristics sorbent, crowding surface results leading strong aggregation tendency (1-40). [Diagram: see text] CD spectra pH 7: A) solution ([Abeta]=0.2 mg.ml(-1)) freshly prepared (line) overnight incubation (symbols);B) (Gamma=0.5 mg.m(-2)).