Altering peptide fibrillization by polymer conjugation
Hamley, Ian W.
- Publisher: American Chemical Society
A strategy is presented that exploits the ability of\ud synthetic polymers of different nature to disturb the strong selfassembly\ud capabilities of amyloid based β-sheet forming peptides.\ud Following a convergent approach, the peptides of interest were\ud synthesized via solid-phase peptide synthesis (SPPS) and the\ud polymers via reversible addition−fragmentation chain transfer\ud (RAFT) polymerization, followed by a copper(I) catalyzed azide−\ud alkyne cycloaddition (CuAAC) to generate the desired peptide−\ud polymer conjugates. This study focuses on a modified version of\ud the core sequence of the β-amyloid peptide (Aβ), Aβ(16−20) (KLVFF). The influence of attaching short poly(Nisopropylacrylamide)\ud and poly(hydroxyethylacrylate) to the peptide sequences on the self-assembly properties of the hybrid\ud materials were studied via infrared spectroscopy, TEM, circular dichroism and SAXS. The findings indicate that attaching these\ud polymers disturbs the strong self-assembly properties of the biomolecules to a certain degree and permits to influence the\ud aggregation of the peptides based on their β-sheets forming abilities. This study presents an innovative route toward targeted and\ud controlled assembly of amyloid-like fibers to drive the formation of polymeric nanomaterials.
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