Record number :
1248550
Title of article :
Quaternary Structure of a Mature Amyloid Fibril from Alzheimer’s Aβ(1-40) Peptide
Author/Authors :
Carsten Sachse، نويسنده , , Chen Xu، نويسنده , , Karin Wieligmann، نويسنده , , Stephan Diekmann، نويسنده , , Ludmila Kolmakova-Partensky and Nikolaus Grigorieff، نويسنده , , Marcus F?ndrich، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2006
Pages :
8
From page :
347
To page :
354
Abstract :
Amyloid fibrils are fibrous polypeptide aggregates that can be formed in vitro and under pathologic conditions, such as in type II diabetes, Alzheimerʹs and Creutzfeldt-Jakob diseases. Using a range of biophysical techniques including electron microscopy we have analysed the quaternary structure of a mature amyloid fibril formed from the Aβ(1-40) peptide from Alzheimerʹs disease. We find that the analysed fibril is discernibly polar and represents a left-handed helix consisting of two or three protofilaments. These are organised in a manner so that the cross-section is, under the present resolution conditions (2.6 nm), S-shaped. In the cross-section, each protofilament can accommodate two β-strands, suggesting that each protofilament contains two cross-β-sheets. These data shed new light on the way in which Aβ(1-40) and the protofilaments formed from this peptide are organised within the mature fibril.
Keywords :
Aggregates , neurodegeneration , Protein folding , Prion
Journal title :
Journal of Molecular Biology
Serial Year :
2006
Link To Document :
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