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An FT-IR study of the beta-amyloid conformation: standardization of aggregation grade.

Abstract：

:The aggregation of beta-amyloid peptides is very important for their neurotoxic effect; standardization of the aggregation grade is necessary for biological experiments. Measurement of aggregation with physicochemical methods is a difficult task. The present work revealed that FT-IR can be used for studying the aggregation properties of beta-amyloid peptides and the effects of environmental variables (solvent, pH, ions, and temperature) on aggregation. In dimethyl sulfoxide or hexafluoroisopropanol, amyloid peptides are in a monomeric state; on dilution with phosphate buffer just before measurement is made, aggregation begins. A detailed two-dimensional FT-IR correlation spectroscopic study was made of the conformational transitions that occur during the aggregation of beta-amyloid peptides. Two processes (random/helix-to-beta-sheet and aggregation of beta-sheets) and multiple conformational states were observed before the most stable form was attained. beta-Amyloid peptides undergo decomposition in basic buffers containing Ca(2+); this process should be avoided during aging experiments.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Szabó Z,Klement E,Jost K,Zarándi M,Soós K,Penke B

doi

10.1006/bbrc.1999.1667

subject

Has Abstract

pub_date

1999-11-19 00:00:00

pages

297-300

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(99)91667-4

journal_volume

265

pub_type

杂志文章

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