Solution self-assembly of hybrid block copolymers containing poly(ethylene glycol) and amphiphilic peptide sequences
The self-assembly in aqueous solution of hybrid block copolymers consisting of amphiphilic ?-strand peptide sequences flanked by one or two PEG chains was investigated by means of circular dichroism spectroscopy, small-angle X-ray scattering, and transmission electron microscopy. In comparison with the native peptide sequence, it was found that the peptide secondary structure was stabilized against pH variation in the di- and tri-block copolymers with PEG. Small-angle X-ray scattering indicated the presence of fibrillar structures, the dimensions of which are comparable to the estimated width of a ?-strand (with terminal PEG chains in the case of the copolymers). Transmission electron microscopy on selectively stained and dried specimens shows directly the presence of fibrils. It is proposed that these fibrils result from the hierarchical self-assembly of peptide ?-strands into helical tapes, which then stack into fibrils. © 2005 American Chemical Society.
Keywords: Cells ; Molecular structure ; Polyethylene glycols ; Polypeptides ; Self assembly ; Solutions ; Transmission electron microscopy ; X ray scattering ; Circular dichroism ; Fibrils ; Hybrid block copolymers ; Peptide sequences ; Block copolymers ; amyloid beta protein ; macrogol
Record created on 2005-07-07, modified on 2016-08-08