title: Membrane-Induced Dichotomous Conformation of Amyloid β with the Disordered N-Terminal Segment Followed by the Stable C-Terminal β Structure.
abstract: Various neurodegenerative disorders are ascribed to pathogenic molecular processes involving conformational transitions of amyloidogenic proteins into toxic aggregates characterized by their β structures. Accumulating evidence indicates that neuronal cell membranes provide platforms for such conformational transitions of pathogenic proteins as best exemplified by amyloid β (Aβ). Therefore, membrane-bound Aβ species can be promising targets for the development of novel drugs for Alzheimer's disease. In the present study, solid-state nuclear magnetic resonance spectroscopy has elucidated the membrane-induced conformation of Aβ, in which the disordered N-terminal segment is followed by the stable C-terminal β strand. The data provides an insight into the molecular processes of the conformational transition of Aβ coupled with its assembly into parallel β structures.
authors.affiliation: Okazaki Institute for Integrative Bioscience, National Institutes of Natural Sciences, Okazaki, 444-8787, Japan.|Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya, 467-8603, Japan.
authors.forename: Maho
authors.initials: M
authors.lastname: Yagi-Utsumi
authors.affiliation: Okazaki Institute for Integrative Bioscience, National Institutes of Natural Sciences, Okazaki, 444-8787, Japan.|Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya, 467-8603, Japan.
authors.forename: Koichi
authors.initials: K
authors.lastname: Kato
authors.affiliation: Institute for Molecular Science, National Institutes of Natural Sciences, Okazaki, 444-8585, Japan.
authors.forename: Katsuyuki
authors.initials: K
authors.lastname: Nishimura
mesh_terms: D000544:Alzheimer Disease / Q000378:metabolism*; D016229:Amyloid beta-Peptides / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism*; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D010446:Peptide Fragments / Q000378:metabolism; D011487:Protein Conformation; D017510:Protein Folding
chemical_list: D016229:Amyloid beta-Peptides; D010446:Peptide Fragments