1 research outputs found
Altering Peptide Fibrillization by Polymer Conjugation
A strategy is presented that exploits the ability of
synthetic
polymers of different nature to disturb the strong self-assembly capabilities
of amyloid based β-sheet forming peptides. Following a convergent
approach, the peptides of interest were synthesized via solid-phase
peptide synthesis (SPPS) and the polymers via reversible addition–fragmentation
chain transfer (RAFT) polymerization, followed by a copper(I) catalyzed
azide–alkyne cycloaddition (CuAAC) to generate the desired
peptide–polymer conjugates. This study focuses on a modified
version of the core sequence of the β-amyloid peptide (Aβ),
Aβ(16–20) (KLVFF). The influence of attaching short poly(<i>N</i>-isopropylacrylamide) and poly(hydroxyethylacrylate) to
the peptide sequences on the self-assembly properties of the hybrid
materials were studied via infrared spectroscopy, TEM, circular dichroism
and SAXS. The findings indicate that attaching these polymers disturbs
the strong self-assembly properties of the biomolecules to a certain
degree and permits to influence the aggregation of the peptides based
on their β-sheets forming abilities. This study presents an
innovative route toward targeted and controlled assembly of amyloid-like
fibers to drive the formation of polymeric nanomaterials