Solution structures of Alzheimeras amyloid A beta sub(13-23) peptide: NMR studies in solution and in SDS

To be believed that interaction of amyloid peptides with the cellular membrane is one of the mechanisms for the neurotoxicity of A beta . Therefore, structural studies of beta-amyloid in solution and in a apeptideabio-membranea complex are of intense interest. The aim of this study was to acquire a better understanding of the mechanism of "A beta peptideamicelle surface" complex formation. Previous studies of A beta peptides binding on the micelle surface show the presence of helical region between 15a24 residues and that fragment between 11-28 residues have a tendency to exit the hydrophobic environment of the micelle core and to bind to the micelle surface. In present paper we considered the fragment of A beta from 13 to 23 residues and found that L17, F19 and F20 residues region play a great role in the process of binding of A beta to the micelle surface.