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Stimulation and inhibition of fibril formation by a peptide in the presence of different concentrations of SDS
Author(s) -
Pertinhez Thelma A,
Bouchard Mario,
Smith Richard A.G,
Dobson Christopher M,
Smith Lorna J
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03333-1
Subject(s) - fibril , peptide , chemistry , biophysics , micelle , membrane , sodium dodecyl sulfate , critical micelle concentration , aqueous solution , biochemistry , organic chemistry , biology
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.