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

FEBS Letters

Smith, Richard A.G¹  Dobson, Christopher M²  Smith, Lorna J²  Pertinhez, Thelma A²  Bouchard, Mario² 

[1] Adprotech Ltd., Chesterford Research Park, Little Chesterford, Saffron Walden Essex, UK;Oxford Centre for Molecular Sciences, Central Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QH, UK

关键词: Peptide;    Sodium dodecyl sulphate;    Amyloid fibrils;    Circular dichroism;    Electron microscopy;    CD;    circular dichroism;    cmc;    critical micellar concentration;    EM;    electron microscopy;    SDS;    sodium dodecyl sulphate;   

DOI  :  10.1016/S0014-5793(02)03333-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown