title: Surfactant-induced conformational transition of amyloid beta-peptide.
abstract: Accumulating evidence suggests that Abeta(1-42)-membrane interactions may play an important role in the pathogenesis of Alzheimer's disease. However, the mechanism of this structural transition remains unknown. In this work, we have shown that submicellar concentrations of sodium dodecyl sulfate (SDS) can provide a minimal platform for Abeta(1-42) self-assembly. To further investigate the relation between Abeta(1-42) structure and function, we analyzed peptide conformation and aggregation at various SDS concentrations using circular dichroism (CD), Fourier transform infrared spectroscopy, and gel electrophoresis. These aggregates, as observed via atomic force microscopy, appeared as globular particles in submicellar SDS with diameters of 35-60 nm. Upon sonication, these particles increased in disc diameter to 100 nm. Pyrene I (3)/I (1) ratios and 1-anilinonaphthalene-8-sulfonic acid binding studies indicated that the peptide interior is more hydrophobic than the SDS micelle interior. We have also used Forster resonance energy transfer between N-terminal labeled pyrene and tyrosine (10) of Abeta(1-42) in various SDS concentrations for conformational analysis. The results demonstrate that SDS at submicellar concentrations accelerates the formation of spherical aggregates, which act as niduses to form large spherical aggregates upon sonication.
authors.affiliation: Bio-Organic and Neurochemistry Laboratory, Central Leather Research Institute, Adyar, Chennai, 600 020, India. nsureshh@gmail.com
authors.forename: N
authors.initials: N
authors.lastname: Sureshbabu
authors.forename: R
authors.initials: R
authors.lastname: Kirubagaran
authors.forename: R
authors.initials: R
authors.lastname: Jayakumar
mesh_terms: D020106:Acrylamide; D016229:Amyloid beta-Peptides / Q000737:chemistry*; D015153:Blotting, Western; D002942:Circular Dichroism; D004553:Electric Conductivity; D004591:Electrophoresis, Polyacrylamide Gel; D005453:Fluorescence; D031541:Fluorescence Resonance Energy Transfer; D057927:Hydrophobic and Hydrophilic Interactions; D018625:Microscopy, Atomic Force; D008958:Models, Molecular; D010446:Peptide Fragments / Q000737:chemistry*; D011487:Protein Conformation / Q000187:drug effects*; D012967:Sodium Dodecyl Sulfate / Q000737:chemistry*; D013010:Sonication; D017550:Spectroscopy, Fourier Transform Infrared; D013501:Surface-Active Agents / Q000737:chemistry*
chemical_list: D016229:Amyloid beta-Peptides; D010446:Peptide Fragments; D013501:Surface-Active Agents; C075222:amyloid beta-protein (1-42); D020106:Acrylamide; D012967:Sodium Dodecyl Sulfate