Amyloid-induced aggregation and precipitation of soluble proteins: an electrostatic contribution of the Alzheimer's beta (25-35) amyloid fibril
Biochemistry 40(7): 2148-2154
ISSN/ISBN: 0006-2960 PMID: 11329283 DOI: 10.1021/bi002156h
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.