Altering peptide fibrillization by polymer conjugation

Dehn, S., Castelletto, V., Hamley, I. W. ORCID: https://orcid.org/0000-0002-4549-0926 and Perrier, S. (2012) Altering peptide fibrillization by polymer conjugation. Biomacromolecules, 13 (9). pp. 2739-2747. ISSN 1525-7797 doi: 10.1021/bm3007117

Abstract/Summary

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
URI	https://reading-clone.eprints-hosting.org/id/eprint/29261
Identification Number/DOI	10.1021/bm3007117
Refereed	Yes
Divisions	Interdisciplinary centres and themes > Chemical Analysis Facility (CAF) Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
Publisher	American Chemical Society
Download/View statistics	View download statistics for this item