NDLI: Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution.

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Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution.

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Year: 1993 Volume: 2 Issue: 2

Year: 1993 Volume: 2 Issue: 1

Year: 1992 Volume: 1

Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	LeVine, H.
Description	Author Affiliation: LeVine H ( Department of Neuroscience Pharmacology, Parke-Davis Pharmaceutical Research Division, Warner-Lambert Company, Ann Arbor, Michigan 48106-1047.)
Abstract	Thioflavine T (ThT) associates rapidly with aggregated fibrils of the synthetic beta/A4-derived peptides beta(1-28) and beta(1-40), giving rise to a new excitation (ex) (absorption) maximum at 450 nm and enhanced emission (em) at 482 nm, as opposed to the 385 nm (ex) and 445 nm (em) of the free dye. This change is dependent on the aggregated state as monomeric or dimeric peptides do not react, and guanidine dissociation of aggregates destroys the signal. There was no effect of high salt concentrations. Binding to the beta(1-40) is of lower affinity, Kd 2 microM, while it saturates with a Kd of 0.54 microM for beta(1-28). Insulin fibrils converted to a beta-sheet conformation fluoresce intensely with ThT. A variety of polyhydroxy, polyanionic, or polycationic materials fail to interact or impede interaction with the amyloid peptides. This fluorometric technique should allow the kinetic elucidation of the amyloid fibril assembly process as well as the testing of agents that might modulate their assembly or disassembly.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	3
Volume Number	2
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1993-03-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Amyloid Beta-peptides Metabolism Thiazoles Amino Acid Sequence Chemical Synthesis Chemistry Fluorescent Dyes Hydrogen-ion Concentration In Vitro Techniques Kinetics Molecular Sequence Data Molecular Structure Protein Conformation Spectrometry, Fluorescence Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution.

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Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution.

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