Transforming protein-polymer conjugate purification by tuning protein solubility

Stefanie L. Baker, Aravinda Munasinghe, Bibifatima Kaupbayeva, Nin Rebecca Kang, Marie Certiat, Hironobu Murata, Krzysztof Matyjaszewski, Ping Lin, Coray M. Colina and Alan J. Russell ()
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Stefanie L. Baker: Carnegie Mellon University
Aravinda Munasinghe: University of Florida
Bibifatima Kaupbayeva: Carnegie Mellon University
Nin Rebecca Kang: Carnegie Mellon University
Marie Certiat: University of Florida
Hironobu Murata: Carnegie Mellon University
Krzysztof Matyjaszewski: Carnegie Mellon University
Ping Lin: University of Florida
Coray M. Colina: University of Florida
Alan J. Russell: Carnegie Mellon University

Nature Communications, 2019, vol. 10, issue 1, 1-12

Abstract: Abstract Almost all commercial proteins are purified using ammonium sulfate precipitation. Protein-polymer conjugates are synthesized from pure starting materials, and the struggle to separate conjugates from polymer, native protein, and from isomers has vexed scientists for decades. We have discovered that covalent polymer attachment has a transformational effect on protein solubility in salt solutions. Here, protein-polymer conjugates with a variety of polymers, grafting densities, and polymer lengths are generated using atom transfer radical polymerization. Charged polymers increase conjugate solubility in ammonium sulfate and completely prevent precipitation even at 100% saturation. Atomistic molecular dynamic simulations show the impact is driven by an anti-polyelectrolyte effect from zwitterionic polymers. Uncharged polymers exhibit polymer length-dependent decreased solubility. The differences in salting-out are then used to simply purify mixtures of conjugates and native proteins into single species. Increasing protein solubility in salt solutions through polymer conjugation could lead to many new applications of protein-polymer conjugates.

Date: 2019
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DOI: 10.1038/s41467-019-12612-9

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