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Solid-phase synthesis of protein-polymers on reversible immobilization supports

Hironobu Murata, Sheiliza Carmali, Stefanie L. Baker, Krzysztof Matyjaszewski and Alan J. Russell ()
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Hironobu Murata: Carnegie Mellon University
Sheiliza Carmali: Carnegie Mellon University
Stefanie L. Baker: Carnegie Mellon University
Krzysztof Matyjaszewski: Carnegie Mellon University
Alan J. Russell: Carnegie Mellon University

Nature Communications, 2018, vol. 9, issue 1, 1-10

Abstract: Abstract Facile automated biomacromolecule synthesis is at the heart of blending synthetic and biologic worlds. Full access to abiotic/biotic synthetic diversity first occurred when chemistry was developed to grow nucleic acids and peptides from reversibly immobilized precursors. Protein–polymer conjugates, however, have always been synthesized in solution in multi-step, multi-day processes that couple innovative chemistry with challenging purification. Here we report the generation of protein–polymer hybrids synthesized by protein-ATRP on reversible immobilization supports (PARIS). We utilized modified agarose beads to covalently and reversibly couple to proteins in amino-specific reactions. We then modified reversibly immobilized proteins with protein-reactive ATRP initiators and, after ATRP, we released and analyzed the protein polymers. The activity and stability of PARIS-synthesized and solution-synthesized conjugates demonstrated that PARIS was an effective, rapid, and simple method to generate protein–polymer conjugates. Automation of PARIS significantly reduced synthesis/purification timelines, thereby opening a path to changing how to generate protein–polymer conjugates.

Date: 2018
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-03153-8

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DOI: 10.1038/s41467-018-03153-8

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