4.4 Article

A weakly clustered n terminus inhibits Aβ(1-40) amyloidogenesis

Journal

CHEMBIOCHEM
Volume 7, Issue 11, Pages 1662-+

Publisher

WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.200600270

Keywords

amyloidogenesis; beta-amyloid; NMR spectroscopy; protein folding; protein structures

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Take pills for stability? A partly structured N terminus was detected in the beta-amyloid (1-40) peptide by using dynamic NMR studies. This partly N terminus (residues 5-16; shown here) was disrupted under amyloidogenic conditions (high temperature, low pH, and in the presence of Zn2+ ions). The results suggest that destabilization of this cluster might be a key step in A beta amyloidogenesis.

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