title: Stimulation and inhibition of fibril formation by a peptide in the presence of different concentrations of SDS.
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 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.
authors.affiliation: Oxford Centre for Molecular Sciences, Central Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QH, UK.
authors.forename: Thelma A
authors.initials: TA
authors.lastname: Pertinhez
authors.forename: Mario
authors.initials: M
authors.lastname: Bouchard
authors.forename: Richard A G
authors.initials: RA
authors.lastname: Smith
authors.forename: Christopher M
authors.initials: CM
authors.lastname: Dobson
authors.forename: Lorna J
authors.initials: LJ
authors.lastname: Smith
mesh_terms: D002942:Circular Dichroism; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D012967:Sodium Dodecyl Sulfate / Q000737:chemistry*; D014867:Water
chemical_list: D010455:Peptides; D014867:Water; D012967:Sodium Dodecyl Sulfate