Abstract
The formation of amyloid fibrils is one of the variants of the self-organization of polypeptide chains. For the amyloid aggregation, the solution must be oversaturated with proteins. The interface of the liquid (solution) and solid (vessel walls) phases can trigger the adsorption of protein molecules, and the resulting oversaturation can initiate conformational transitions in them. In any laboratory experiment, we cannot exclude the presence of surfaces such as the walls of vessels, cuvettes, etc. However, in many works devoted to the study of amyloid formation, this feature is not considered. In our work, we investigated the behavior of the Aβ 1-40 peptide at the water–glass, water–quartz, and water–plastic interface. We carried out a series of simple experiments and showed that the Aβ 1-40 peptide is actively adsorbed on these surfaces, which leads to a significant interaction and aggregation of peptides. This means that the interface can be the place where the first amyloid nucleus appears. We suggest that this effect may also be one of the reasons for the difficulty of reproducing kinetic data when studying the aggregation of the amyloid of the Aβ 1-40 peptide and other amyloidogenic proteins
Highlights
We have shown that Aβ 1-40 peptide is adsorbed in significant
Results and Discussion amounts on the glass surface, which leads to the significant interaction and aggregation
Since study 3ofshow amyloid aggregation is carried outadsorbed inon glass and in plastic tubesredirected and in quartzour cuvettes, we investigated the influence these washed off
Summary
Publisher’s Note: MDPI stays neutral with regard to jurisdictional claims in published maps and institutional affiliations. The formation of the nucleus of amyloid fibrils Many researchers suggest their spontaneous appearance in solution [1,2]. Studies devoted to the effect of various surfaces on amyloid formation indicate similar phenomena during the initiation of the amyloid fibrils growth [6,7,8]. The area of interest of the presented work was the effect of the surface of the vessel, cuvette, or test tube, in which amyloid aggregates are formed. In this closer fluorescence energy of Cy3 can transfer to Cy5 This effect allows to evaluate the case, we used two dyes that form a FRET pair—Cy3 and Cy5.
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