Abstract
Elaborate morphology: The αSβ1 peptide, a fragment of α-synuclein, assembles into flat tapes consisting of a peptide bilayer, which can be modeled based on the cross-β structure found in amyloid proteins. The tapes are stabilized by hydrogen bonding, whilst the amphiphilic nature of the peptide results in the thin bilayer structure. To further stabilize the structure, these tapes may twist to form helical tapes, which subsequently close into nanotubes.
Highlights
A number of short peptides and larger proteins are able to self-assemble to form cross-b amyloid-like fibrils.[1]
A-Synuclein (a-syn) is a 140-residue peptide that assembles to form amyloid-like fibrils that are deposited in Lewy bodies in Parkinsons disease.[3] a-Syn fibrils assembled in vitro have been confirmed to have a b-sheet-rich structure consistent with the amyloid cross-b architecture.[7]
Solid-state NMR studies on the cross-b amyloid core of recombinant human a-syn fibrils have indicated sets of b-strands at discrete positions between 30–110.[8]. We have explored the assembly potential and structure of a segment of a-syn corresponding to positions 37–44 (NH2-VLYVGSKT-COOH) referred to aSb1
Summary
A number of short peptides and larger proteins are able to self-assemble to form cross-b amyloid-like fibrils.[1]. P. Sikorski Department of Physics, Norwegian University of Science and Technology, Trondheim (Norway)
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