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Self-assembly of Telechelic Tyrosine End-Capped PEO Star polymers in Aqueous Solution

DOI: 10.1021/acs.biomac.7b01420 DOI Help

Authors: Charlotte J. C. Edwards-gayle (University of Reading) , Francesca Greco (University of Reading) , Ian W. Hamley (Diamond Light Source) , Robert P. Rambo (Diamond Light Source) , Mehedi Reza (Aalto University) , Janne Ruokolainen (Aalto University) , Dimitrios Skoulas (University of Athens) , Hermis Iatrou (University of Athens)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Biomacromolecules

State: Published (Approved)
Published: December 2017
Diamond Proposal Number(s): 14684 , 15778

Abstract: 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 (NCA)-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 (SAXS) and cryogenic transmission electron microscopy (Cryo-TEM). In contrast to previous studies on linear telechelic PEO-oligotyrosine conjugates which show self-assembly into -sheet fibrils, the star architecture suppresses fibril formation and instead micelles are generally observed, a small population of fibrils only being observed upon pH adjustment. Hydrogelation is also suppressed by the polymer star architecture. However, hydrogels can be produce by addition of sodium alginate with calcium chloride. These peptide-functionalized star polymer solutions are cytocompatible at sufficiently low concentration. These polymers present tyrosine at high density and may be useful in the development of future enzyme or pH-responsive biomaterials.

Subject Areas: Chemistry

Instruments: B21-High Throughput SAXS

Other Facilities: ESRF

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