Self-Assembly of PEGylated Peptide Conjugates Containing a Modified Amyloid β-Peptide Fragment

The self-assembly of PEGylated peptides containing a modified sequence from the amyloid β peptide, FFKLVFF, has been studied in aqueous solution. PEG molar masses PEG1k, PEG2k, and PEG10k were used in the conjugates. It is shown that the three FFKLVFF-PEG hybrids form fibrils comprising a FFKLVFF core and a PEG corona. The β-sheet secondary structure of the peptide is retained in the FFKLVFF fibril core. At sufficiently high concentrations, FFKLVFF-PEG1k and FFKLVFF-PEG2k form a nematic phase, while PEG10k-FFKLVFF exhibits a hexagonal columnar phase. Simultaneous small angle neutron scattering/shear flow experiments were performed to study the shear flow alignment of the nematic and hexagonal liquid crystal phases. On drying, PEG crystallization occurs without disruption of the FFKLVFF β-sheet structure leading to characteristic peaks in the X-ray diffraction pattern and FTIR spectra. The stability of β-sheet structures was also studied in blends of FFKLVFF-PEG conjugates with poly(acrylic acid) (PAA). While PEG crystallization is only observed up to 25% PAA content in the blends, the FFKLVFF β-sheet structure is retained up to 75% PAA.