The search for ability to manage the formation of amyloid fibrils is the goal of many studies. To stop and initiate the growth process of amyloid fibrils of the A-beta peptide, mutant peptides with key amino acid substitutions to proline were designed. To investigate the mechanism of action of these peptides, a hybrid construction based on the thermostable hexameric Hfq protein to which these peptides are attached was designed. This fusion protein was obtained, isolated and purified. Its stability and ability to aggregate on heating was tested. The results of the experiments confirm the hypotheses of high stability and resistance to aggregation of the obtained structure in comparison with the thioredoxin-based hybrid protein that was used previously. These results will allow us to use the developed design in studies of amyloid formation.
Hfq, amyloid formation, hybrid proteins, protein engineering, thioredoxin, Hfq
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