Structure of the β-Amyloid (10-35) Fibril. Int. J. Exp. Clin. In V est, 5(121), 1998.

Structure of the β-Amyloid (10-35) Fibril.
Int. J. Exp. Clin. In V est, 5(121), 1998.
T. Burkoth, T. Benzinger, V. Urban, D. Morgan, D. Gregory, P. Thiyagarajan, R. Botto, S. Meredith, and D. Lynn.

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Abstract: The primary component of the amyloid plaques in Alzheimer’s disease (AD) is a highly ordered fibril composed of the 39-43 amino acid peptide, �-amyloid (A�). The presence of this fibril has been correlated
with both the onset and severity of the disease. Using a combination of synthetic model peptides, solid-state NMR, electron microscopy, and small angle neutron scattering (SANS), methods that allowed fibrils to be studied directly both in solution and in the solid state, the three-dimensional structure of fibrils formed from A�(10-35) is assigned. The structure consists of six laminated �-sheets propagating and twisting along the fibril axis. Each peptide strand is oriented perpendicular to the helical axis in a parallel �-sheet, with each like amino acid residue in register along the sheet. The six sheets are laminated, probably also in parallel arrays, to give a fibril with dimensions of about 60 × 80 Å. Both the methodology developed and the structural insight gained here lay the foundation for strategies to characterize and design materials capable of amyloid- like self-assembly.

Aβの10-35領域は単体で自己集合。1-10は親水的。
この部分だけとってきて集合させ、構造を解析した。PEG付けた。
どうやらパラレルに重合。アミノ酸側鎖パッキング

一個ぺこって付くと10 Åのびるので、10 μmになるには10000 mer必要*1

*1:ここら不安あり