Conformational transitions as origin of peptide aggregation are considered as a fundamental molecular event in early processes of degenerative diseases. A detailed investigation of these processes is hampered by intrinsic problems such as high tendency of the involved peptides for beta-sheet formation and spontaneous aggregation limiting their experimental accessibility. We have recently developed a new generation of switch-peptides (S-peptides) for the controlled induction of conformational transitions at physiologic pH using O ->N acyl migrations in situ. Here, we explore the sequential triggering of O ->N acyl migrations in amyloid beta derived switch-peptides as a general tool to study the onset and inhibition of polypeptide folding, self-assembly and aggregation (Fig. 1).
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