Stimulation and inhibition of fibril formation by a peptide in the presence of different concentrations of SDS.
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 alpha-helical but converts rapidly to a beta-sheet structure and large quantities of fibrils form. In SDS above the critical micellar concentration the peptide adopts a stable alpha-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.
Pertinhez
Thelma A
TA
Oxford Centre for Molecular Sciences, Central Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QH, UK.
Bouchard
Mario
M
Smith
Richard A G
RA
Dobson
Christopher M
CM
Smith
Lorna J
LJ
D002942:Circular Dichroism; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D012967:Sodium Dodecyl Sulfate / Q000737:chemistry*; D014867:Water
D010455:Peptides; D014867:Water; D012967:Sodium Dodecyl Sulfate