American Chemical Society
bm3007117_si_001.pdf (1.7 MB)

Altering Peptide Fibrillization by Polymer Conjugation

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journal contribution
posted on 2012-09-10, 00:00 authored by Sabrina Dehn, Valeria Castelletto, Ian W. Hamley, Sébastien Perrier
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(N-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.