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Altering peptide fibrillization by polymer conjugation

Dehn, S., Castelletto, V., Hamley, I. W. ORCID: and Perrier, S. (2012) Altering peptide fibrillization by polymer conjugation. Biomacromolecules, 13 (9). pp. 2739-2747. ISSN 1525-7797

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To link to this item DOI: 10.1021/bm3007117


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.

Item Type:Article
Divisions:Interdisciplinary centres and themes > Chemical Analysis Facility (CAF)
Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
ID Code:29261
Publisher:American Chemical Society


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