Conformational change of a synthetic amyloid analogue des[Ala21,3O]A42 upon binding to octyl glucoside micelles

Ilona Laczkó-Hollósi, M. Hollósi, Virginia M Y Lee, Henry H. Mantsch

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

The secondary structure of a synthetic amyloid fragment des [Ala21,30]A42 was studied by circular dichroism and Fourier transformed infrared spectroscopy. Measurements were performed in trifluoroethanol/water and octyl β-d-glucopyranoside solutions. The spectra of the peptide in trifluoroethanol indicate a high percentage of a-helical structure. However, in octyl glucoside, at and above the critical micelle concentration, the peptide adopts a β-sheet conformation. Secondary structure analysis yields a predominant (> 70 %) β-sheet content. Our data suggest that the peptide backbone or polar side groups of des[Ala21,30]A42 interact with the sugar-coated surface of micelles, which promotes an a to β conformational transition.

Original languageEnglish
Pages (from-to)345-348
Number of pages4
JournalEuropean Biophysics Journal
Volume21
Issue number5
DOIs
Publication statusPublished - Nov 1992

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Micelles
Amyloid
Trifluoroethanol
Peptides
Circular Dichroism
Spectrum Analysis
Water
octyl-beta-D-glucoside

Keywords

  • Alzheimer's disease
  • Amyloid A4
  • Conformational change
  • Octyl glucoside

ASJC Scopus subject areas

  • Biophysics

Cite this

Conformational change of a synthetic amyloid analogue des[Ala21,3O]A42 upon binding to octyl glucoside micelles. / Laczkó-Hollósi, Ilona; Hollósi, M.; Lee, Virginia M Y; Mantsch, Henry H.

In: European Biophysics Journal, Vol. 21, No. 5, 11.1992, p. 345-348.

Research output: Contribution to journalArticle

Laczkó-Hollósi, Ilona ; Hollósi, M. ; Lee, Virginia M Y ; Mantsch, Henry H. / Conformational change of a synthetic amyloid analogue des[Ala21,3O]A42 upon binding to octyl glucoside micelles. In: European Biophysics Journal. 1992 ; Vol. 21, No. 5. pp. 345-348.
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