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Design of supramolecular β-sheet forming β-turns containing aromatic rings and non-coded α-aminoisobutyric acid and the formation of flat fibrillar structures through self-assembly

Single crystal X-ray diffraction studies show that the three designed tripeptides Boc-Leu-Aib-m-NA-NO2 (I), Boc-Phe-Aib-m-NA-NO2 (II) and Boc-Pro-Aib-m-ABA-OMe (III) (Aib, α-aminoisobutyric acid; m-NA, m-nitroaniline; m-ABA, m-aminobenzoic acid; Boc, t-butyloxycarbonyl) containing aromatic rings in the backbones adopt β-turn structures that are self-assembled through intermolecular hydrogen bonds and van der Waals interactions to create layers of β-sheets. Solvent-dependent NMR titration and CD studies show that the β-turn structures of the peptides also exist in the solution phase. The field emission scanning electron microscopic and transmission electron microscopic images of the peptides in the solid state reveal fibrillar structures of flat morphology that are formed through β-sheet mediated self-assembly of the preorganised β-turn building blocks.