Abstract
The Structure of Cross‐β Tapes and Tubes Formed by an Octapeptide, αSβ1
Highlights
X-ray fiber diffraction has been extensively used to reveal that many proteins and peptides are able to assemble to form a cross-b structure in which b-strands run perpendicular to the fiber axis and associate to form long-range hydrogen-bonded b-sheets.[1c,4] The inherent strength of this arrangement is underlined by the similarity to the architecture of cross-b silks.[4a,5] The non-covalent self-assembly of peptide monomers underpins the spontaneous formation of elaborate fibrillar structures.[6]
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
X-ray fiber diffraction has been extensively used to reveal that many proteins and peptides are able to assemble to form a cross-b structure in which b-strands run perpendicular to the fiber axis and associate to form long-range hydrogen-bonded b-sheets.[1c,4] The inherent strength of this arrangement is underlined by the similarity to the architecture of cross-b silks.[4a,5] The non-covalent self-assembly of peptide monomers underpins the spontaneous formation of elaborate fibrillar structures.[6]. P. Sikorski Department of Physics, Norwegian University of Science and Technology, Trondheim (Norway)
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