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    ATRP under Biologically Relevant Conditions: Grafting from a Protein
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    † Department of Chemistry, Carnegie Mellon University, 4400 Fifth Avenue, Pittsburgh, Pennsylvania 15213, United States
    § Department of Chemistry, Franklin and Marshall College, Lancaster, Pennsylvania 17604-3003, United States
    *E-mail: [email protected]
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    ACS Macro Letters

    Cite this: ACS Macro Lett. 2012, 1, 1, 6–10
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    https://doi.org/10.1021/mz200020c
    Published November 9, 2011
    Copyright © 2011 American Chemical Society
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    Abstract

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    Atom transfer radical polymerization (ATRP) methods were developed in water-based media, to grow polymers from proteins under biologically relevant conditions. These conditions gave good control over the resulting polymers, while still preserving the protein’s native structure. Several reaction parameters, such as ligand structure, halide species, and initiation mode were optimized in water and PBS buffer to yield well-defined polymers grown from bovine serum albumin (BSA), functionalized with cleavable ATRP initiators (I). The CuCl complex with ligand 2,2′-bipyridyne (bpy) provides the best conditions for the polymerization of oligo(ethylene oxide) methacrylate (OEOMA) in water at 30 °C under normal ATRP conditions (I/CuCl/CuCl2/bpy = 1/1/9/22), while the CuBr/bpy complex gave better performance in PBS. Activators generated by electron transfer (AGET) ATRP gave well-controlled polymerization of OEOMA at 30 °C with the ligand tris(2-pyridylmethyl)amine (TPMA), (I/CuBr2/TPMA = 1/10/11). The AGET ATRP reactions required slow feeding of a very small amount of ascorbic acid into the aqueous reaction medium or buffer. The reaction conditions developed were used to create a smart, thermoresponsive, protein–polymer hybrid.

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    Cite this: ACS Macro Lett. 2012, 1, 1, 6–10
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