Stimulation and inhibition of fibril formation by a peptide in the presence of different concentrations of SDS

Thelma A. Pertinhez, Mario Bouchard, Richard A G Smith, Christopher M. Dobson, Lorna J. Smith

Research output: Contribution to journalArticle

Abstract

Sodium dodecyl sulphate (SDS), a detergent that mimics some characteristics of biological membranes, has been found to affect significantly fibril formation by a peptide from human complement receptor 1. In aqueous solution the peptide is unfolded but slowly aggregates to form fibrils. In sub-micellar concentrations of SDS the peptide is initially α-helical but converts rapidly to a β-sheet structure and large quantities of fibrils form. In SDS above the critical micellar concentration the peptide adopts a stable α-helical structure and no fibrils are observed. These findings demonstrate the sensitivity of fibril formation to solution conditions and suggest a possible role for membrane components in amyloid fibril formation in living systems.

Original languageEnglish
Pages (from-to)193-197
Number of pages5
JournalFEBS Letters
Volume529
Issue number2-3
DOIs
Publication statusPublished - Oct 9 2002

Keywords

  • Amyloid fibrils
  • Circular dichroism
  • Electron microscopy
  • Peptide
  • Sodium dodecyl sulphate

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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