期刊
CHEMBIOCHEM
卷 16, 期 4, 页码 659-669出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.201402595
关键词
amyloid beta-peptides; diffusion ordered spectroscopy; NMR spectroscopy; relaxation measurements; saturation transfer difference
资金
- Schweizerische Nationalfonds (SNF)
Amyloid- (A) peptide is the major component found in senile plaques of Alzheimer's disease patients. The 42-residue fragment A(1-42) is proposed to be one of the most pathogenic species therein. Here, the soluble A(1-42) species were analyzed by various liquid-state NMR methods. Transient formation of a micelle species was observed at the onset of the aggregation kinetics. This micelle is dissolved after approximately one day. Subsequent loss of this species and the formation of protofibrils are proposed to be the route of fibril formation. Consequently, the observed micelle species is suggested to be on an off-pathway mechanism. Furthermore, characterization of the NMR-observable soluble species shows that it is a random-coil-like entity with low propensities for four -strands. These -strands correlate with the -strand segments observed in A fibrils. This finding indicates that the 3D structure of the fibrils might already be predisposed in the soluble species.
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