Conformational changes of the Amyloid ?Ò-peptide (1-40) adsorbed on solid surfaces

CARLA E. GIACOMELLI; WILLEM NORDE

MACROMOLECULAR BIOSCIENCE

Wiley-VCH

Lugar: Weinheim (Alemania); Año: 2005 vol. 5 p. 401 - 401

1616-5195

font face="AdvP41153C" size="2"> The conformational change of the 39?43 residues of the amyloid b-peptide (Ab) toward a b-sheet enriched state promotes self-aggregation of the peptide molecules and constitutes the major peptide component of the amyloid plaques in Alzheimer patients. The crucial question behind the self-aggregation ofAb is related to the different pathways the peptide may take after cleavage from the amyloid precursor proteins at cellular membranes. This work is aiming at determining the conformation of the Ab (1?40) adsorbed on hydrophobic Teflon and hydrophilic silica particles, as mo