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Membrane-Induced Dichotomous Conformation of Amyloid ? with the Disordered N-Terminal Segment Followed by the Stable C-Terminal ? Structure.

ABSTRACT: Various neurodegenerative disorders are ascribed to pathogenic molecular processes involving conformational transitions of amyloidogenic proteins into toxic aggregates characterized by their ? structures. Accumulating evidence indicates that neuronal cell membranes provide platforms for such conformational transitions of pathogenic proteins as best exemplified by amyloid ? (A?). Therefore, membrane-bound A? 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 A?, in which the disordered N-terminal segment is followed by the stable C-terminal ? strand. The data provides an insight into the molecular processes of the conformational transition of A? coupled with its assembly into parallel ? structures.

SUBMITTER: Yagi-Utsumi M

PROVIDER: S-EPMC4701388 | biostudies-literature | 2016

REPOSITORIES: biostudies-literature

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Membrane-Induced Dichotomous Conformation of Amyloid β with the Disordered N-Terminal Segment Followed by the Stable C-Terminal β Structure.

Yagi-Utsumi Maho M Kato Koichi K Nishimura Katsuyuki K

PloS one 20160105 1

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 disea ...[more]

PMID: 26731546

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