A strategy is presented that exploits the ability of
synthetic polymers of different nature to disturb the strong selfassembly
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(Nisopropylacrylamide)
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
