Charged surfactants induce a non‐fibrillar aggregation pathway of amyloid‐beta peptide |
| |
Authors: | Joana A Loureiro Sandra Rocha Maria do Carmo Pereira |
| |
Institution: | LEPAE, Department of Chemical Engineering, Faculty of Engineering, University of Porto, , Porto, Portugal |
| |
Abstract: | 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. |
| |
Keywords: | beta amyloid surfactants aggregation oligomers Alzheimer |
|
|