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We report a novel self-assembling system of amphiphilic oligopeptides composed of alternating hydrophobic and ionizable amino-acid residues. Three types of peptides, AD12, AE12 and AK12, were prepared as building blocks for this model system. These peptides formed helical conformations in low-concentration solutions, but these peptides adopted β-sheet structures and precipitated in highly concentrated solutions at a pH that neutralizes the charges on the ionizable side chains. In addition, the mixing of the peptides with positive and negative charges on the side chains of the ionizable amino-acid residues was found to trigger the formation of the β-sheet structure. This system could be used to create new materials based on oligopeptides.

polymer journal

Structural studies of amphiphilic oligopeptides composed of alternating alanine and ionizable amino-acid residues using CD and 13C CP/MAS NMR spectroscopy