Self-assembly of an amyloid peptide fragment–PEG conjugate: lyotropic phase formation and influence of PEG crystallization
Castelletto, V., Newby, G. E., Hermida Merino, D., Hamley, I. W., Liu, D. and Noirez, L. (2010) Self-assembly of an amyloid peptide fragment–PEG conjugate: lyotropic phase formation and influence of PEG crystallization. Polymer Chemistry, 1. pp. 453-459. ISSN 1759-9954
Full text not archived in this repository.
To link to this article DOI: 10.1039/b9py00349e
The self-assembly of PEGylated peptides containing a modified sequence from the amyloid beta peptide, YYKLVFF, has been studied in aqueous solution. Two PEG molar masses, PEG1k and PEG3k, were used in the conjugates. It is shown that both YYKLVFF–PEG hybrids form fibrils comprising a peptide core and a PEG corona. The fibrils are much longer for YYKLVFF–PEG1k, pointing to an influence of PEG chain length. The beta-sheet secondary structure of the peptide is retained in the conjugate. Lyotropic liquid crystal phases, specifically nematic and hexagonal columnar phases, are formed at sufficiently high concentration. Flow alignment of these mesophases was investigated by small-angle neutron scattering with in situ steady shearing in a Couette cell. On drying, PEG crystallization occurs leading to characteristic peaks in the X-ray diffraction pattern, and to lamellar structures imaged by atomic force microscopy. The X-ray diffraction pattern retains features of the cross-beta pattern from the beta-sheet structure, showing that this is not disrupted by PEG crystallization.