Self-assembly of telechelic tyrosine end-capped PEO star polymers in aqueous solution

Edwards-Gayle, C. J. C., Greco, F., Hamley, I. W. ORCID: https://orcid.org/0000-0002-4549-0926, Rambo, R. P., Reza, M., Ruokolainen, J., Skoulas, D. and Iatrou, H. (2018) Self-assembly of telechelic tyrosine end-capped PEO star polymers in aqueous solution. Biomacromolecules, 19 (1). pp. 167-177. ISSN 1525-7797 doi: 10.1021/acs.biomac.7b01420

Abstract/Summary

We investigate the self-assembly of two telechelic star polymer–peptide conjugates based on poly(ethylene oxide) (PEO) four-arm star polymers capped with oligotyrosine. The conjugates were prepared via N-carboxy anhydride-mediated ring-opening polymerization from PEO star polymer macroinitiators. Self-assembly occurs above a critical aggregation concentration determined via fluorescence probe assays. Peptide conformation was examined using circular dichroism spectroscopy. The structure of self-assembled aggregates was probed using small-angle X-ray scattering and cryogenic transmission electron microscopy. In contrast to previous studies on linear telechelic PEO–oligotyrosine conjugates that show self-assembly into β-sheet fibrils, the star architecture suppresses fibril formation and micelles are generally observed instead, a small population of fibrils only being observed upon pH adjustment. Hydrogelation is also suppressed by the polymer star architecture. These peptide-functionalized star polymer solutions are cytocompatible at sufficiently low concentration. These systems present tyrosine at high density and may be useful in the development of future enzyme or pH-responsive biomaterials.

Item Type	Article
URI	https://reading-clone.eprints-hosting.org/id/eprint/74705
Item Type	Article
Refereed	Yes
Divisions	Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
Publisher	American Chemical Society
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