Journal
BIOMACROMOLECULES
Volume 13, Issue 9, Pages 2739-2747Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bm3007117
Keywords
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Funding
- ARC [DP1096651]
- EPSRC [EP/F048114/1, EP/G026203/1, EP/G067538/1]
- Engineering and Physical Sciences Research Council [EP/G026203/1, EP/G067538/1, EP/F048114/1] Funding Source: researchfish
- Australian Research Council [DP1096651] Funding Source: Australian Research Council
- EPSRC [EP/F048114/1, EP/G067538/1, EP/G026203/1] Funding Source: UKRI
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A strategy is presented that exploits the ability of synthetic polymers of different nature to disturb the strong self-assembly capabilities of amyloid based beta-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 beta-amyloid peptide (A beta), A beta(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 beta-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.
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