In vitro perturbation of aggregation processes in beta-amyloid peptides: a spectroscopic study

FEBS Lett. 2008 Oct 15;582(23-24):3288-92. doi: 10.1016/j.febslet.2008.08.039. Epub 2008 Sep 19.

Abstract

We have performed an in vitro study to investigate the molecular basis of the aggregation kinetic of 1-40 beta-amyloid peptides (Abeta and the possibility of affecting this aggregation process using an exogenous natural polycyclic pigment, hypericin (Hyp). The effect of Hyp on the self-assembly process at different times of the aggregation kinetic has been investigated utilizing a chaperon-like molecule, alpha-crystallin. Circular dichroism and fluorescence results suggest that Hyp can associate to precursors of the mature fibrils and perturb the aggregation process through intermolecular interactions with the Abeta peptides.

MeSH terms

  • Amyloid beta-Peptides / chemistry*
  • Circular Dichroism
  • Fluorescent Dyes / chemistry*
  • Humans
  • Kinetics
  • Peptide Fragments / chemistry*
  • Perylene / analogs & derivatives*
  • Perylene / chemistry
  • Spectrometry, Fluorescence
  • alpha-Crystallins / chemistry*

Substances

  • Amyloid beta-Peptides
  • Fluorescent Dyes
  • Peptide Fragments
  • alpha-Crystallins
  • amyloid beta-protein (1-40)
  • Perylene
  • hypericin