A Soluble Amyloid Fibril Segment to Study Aggregate Formation

Fibril formation of amyloid proteins involves β‐cross sheet formations and aggregation through hydrophobic interactions. Recently, a soluble amyloid segment has been described which should help to better understand the structural implications and the dynamics of aggregate formation. The approach mig...

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Veröffentlicht in:	ChemMedChem 2007-01, Vol.2 (1), p.47-49
1. Verfasser:	Jaroch, Stefan
Format:	Artikel
Sprache:	eng
Schlagworte:	aggregation Alzheimer Disease - metabolism Alzheimer Disease - pathology Alzheimer's disease Amino Acid Sequence Amyloid - chemistry Amyloid - metabolism amyloids Hydrophobic and Hydrophilic Interactions Models, Chemical Molecular Sequence Data Protein Folding Protein Structure, Secondary Solubility template-assembled synthetic proteins
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Zusammenfassung:	Fibril formation of amyloid proteins involves β‐cross sheet formations and aggregation through hydrophobic interactions. Recently, a soluble amyloid segment has been described which should help to better understand the structural implications and the dynamics of aggregate formation. The approach might be useful to study other protein misfolding processes.
ISSN:	1860-7179 1860-7187
DOI:	10.1002/cmdc.200600222