Premium
Charged surfactants induce a non‐fibrillar aggregation pathway of amyloid‐beta peptide
Author(s) -
Loureiro Joana A.,
Rocha Sandra,
Pereira Maria do Carmo
Publication year - 2013
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.2535
Subject(s) - peptide , thioflavin , chemistry , fibril , amyloid (mycology) , micelle , biophysics , amyloid beta , peptide sequence , pulmonary surfactant , p3 peptide , amino acid , biochemistry , alzheimer's disease , amyloid precursor protein , aqueous solution , organic chemistry , biology , medicine , inorganic chemistry , disease , pathology , gene
The amyloid β‐peptide with a sequence of 42 amino acids is the major constituent of extracellular amyloid deposits in Alzheimer's disease plaques. The control of the peptide self‐assembly is difficult to achieve because the process is fast and is affected by many variables. In this paper, we describe the effect of different charged and non‐charged surfactants on Aβ (1‐42) fibrillation to define common alternate aggregation pathways. The characterization of the peptide‐surfactant interactions by ultra‐structural analysis, thioflavin T assay and secondary structure analysis, suggested that charged surfactants interact with Aβ (1‐42) through electrostatic interactions. Charged micelles slow down the aggregation process and stabilize the peptide in the oligomeric state, whereas non‐charged surfactants promote the Aβ (1‐42) fibril formation. Copyright © 2013 European Peptide Society and John Wiley & Sons, Ltd.