wizyta

od 2020-09-20

Title: Study of molecular mechanisms of amyloid beta-peptid variants aggregation in presence of surfactants

Source: Biophysical Journal

Year : 2016

Abstract:

It is estimated that in 2050 at least 1.25 % of population might have Alzheimer's disease. It is supposed that the most critical changes relevant for the progress of this disease are related to development and deposition of amyloid plaque whose main components are amyloid β-peptides (Aβ).
The aim of this study was characterization of the structure and conformational changes of β-amyloid peptides in the presence of a wide group of surfactants. The kinetic study of the aggregation behavior of different peptides in solution was also undertaken. Four groups of surfactants (cationic, dicationic, tricationic and zwitterionic) and different β-amyloid peptides were selected for the study. The surfactant concentration effect was tested on 1-42 Aβ peptide and its shorter variants (N-terminal with hydrophilic properties and hydrophobic C-terminal fragment).
Analysis of the secondary structure of Aβ peptide in the presence of different concentrations of surfactants as well as a function of temperature, was carried out using FTIR spectroscopy and circular dichroism method. The kinetics of aggregation processes of the peptides and formation of plaques was studied using fluorescence spectroscopy and Thioflavin T assay. The size distribution of aggregates of Aβ peptide was evaluated on the basis of gel electrophoresis.
Results of our study showed different impact of surfactants studied on the conformations of beta-amyloid peptides. Preliminary examination of the cytotoxicity of selected surfactants on HeLa cells was conducted in order to verify their suitability for therapeutic purposes.

DOI: 10.1016/j.bpj.2015.11.2855   (Pobrane:  2020-10-23)