Amyloid Peptide Mixtures: Self-Assembly, Hydrogelation, Nematic Ordering and Catalysts in Aldol Reactions.

Morphological, spectroscopic and scattering studies of the self-assembly and aggregation process of mixtures of [RF]4 and P[RF]4 peptides (where: R = arginine; F = phenylalanine; P = proline), in solution and as hydrogels, were performed to obtain information about polymorphism. CD data confirmed a β-sheet secondary structure conformation for the solutions and TEM images revealed nanofibers with diameters of ~ 10 nm and micrometer lengths. SAXS curves were fitted using a mass fractal-component and a long cylinder shell form factor for the liquid samples, and only a long cylinder shell form factor for the gels. Increasing the P[RF]4 content in the systems leads to a reduction in cylinder radius and core density scattering, suggesting an increase in packing of the peptide molecules; however, the opposite effect was observed for the gels. Remarkably, the gels are birefringent, indicating nematic ordering of the gel fibrils. These compounds show potential as catalysts in the asymmetric aldol reactions, with cyclohexanone and p-nitrobenzaldehyde in aqueous media. A moderate conversion (36.9 %) and a good stereoselectivity (69:31) were observed for the system containing only [RF]4, and with the increase of the P[RF]4, a considerable decrease of the conversion was observed, suggesting differences in the self-assembly and packing factor. Rheological measurements were performed to determine the shear moduli for the soft gels. These model amyloid peptides demonstrate a range of tunable self-assembly behaviors and additionally have potential as biocatalysts.