Section 11
Chapter 10,155

Amyloid-induced aggregation and precipitation of soluble proteins: an electrostatic contribution of the Alzheimer's beta (25-35) amyloid fibril

Konno, T.

Biochemistry 40(7): 2148-2154


ISSN/ISBN: 0006-2960
PMID: 11329283
DOI: 10.1021/bi002156h
Accession: 010154068

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Amyloid-induced aggregation and precipitation of soluble proteins were investigated in vitro using the amyloid fibrils of the beta(25-35) peptide, a cytotoxic fragment of the Alzheimer's beta-peptide at positions 25-35. The aggregation rate of firefly luciferase was found to be modulated by both a chaperone molecule DnaK and the beta(25-35) amyloid, but their effects were opposite in direction. The amyloid fibril drastically facilitated the luciferase aggregation, which may define a kind of anti-chaperone activity. The effect of the beta(25-35) amyloid to promote protein aggregation and precipitation was further demonstrated for a wide variety of target proteins.

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