Search of the physical foundations of the first stages of amyloid aggregation remains an important objective of the protein physics for a last few decades. There are certain analogies between processes amyloid aggregation and crystallization. In both cases, the solution is supersaturated, and the appearance of seed of new phase leads to a cascade of crystallization or protein amyloid fibrils formation. In this work spectral and microscopic investigation of the A-beta peptide aggregation on the glass surface ware done. It is shown experimentally that the glass surface can sorb molecules of A-beta peptide, and thereby lead to an increase in their ability to aggregate, including amyloid. The appearance of phase of protein adsorbed on the surface can affect the aggregation of peptides in bulk solution. The need for taking into account this influence is evident in any study of protein aggregation.
amyloid aggregation, A-beta peptides, nucleation, adsorption
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