An FT-IR study of the β-amyloid conformation: Standardization of aggregation grade

Z. Szabó, É Klement, K. Jost, M. Zarándi, K. Soós, B. Penke

Research output: Article

40 Citations (Scopus)

Abstract

The aggregation of β-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 β-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 β-amyloid peptides. Two processes (random/helix-to-β-sheet and aggregation of β-sheets) and multiple conformational states were observed before the most stable form was attained. β-Amyloid peptides undergo decomposition in basic buffers containing Ca2+; this process should be avoided during aging experiments.

Original languageEnglish
Pages (from-to)297-300
Number of pages4
JournalBiochemical and biophysical research communications
Volume265
Issue number2
DOIs
Publication statusPublished - nov. 19 1999

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ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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