RAFT polymers for protein recognition

Alan F. Tominey, Juila Liese, Sun Wei, Klaus Kowski, Thomas Schrader, Arno Kraft

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Abstract

A new family of linear polymers with pronounced affinity for arginine- and lysine-rich proteins has been created. To this end, N-isopropylacrylamide (NIPAM) was copolymerized in water with a binding monomer and a hydrophobic comonomer using a living radical polymerization (RAFT). The resulting copolymers were water-soluble and displayed narrow polydispersities. They formed tight complexes with basic proteins depending on the nature and amount of the binding monomer as well as on the choice of the added hydrophobic comonomer. © 2010 Tominey et al; licensee Beilstein-Institut.

Original languageEnglish
Article number66
JournalBeilstein Journal of Organic Chemistry
Volume6
DOIs
Publication statusPublished - 17 Jun 2010

Keywords

  • Electrostatic interactions
  • Hydrophobic effect
  • Isothermal calorimetry
  • Protein recognition
  • RAFT polymers

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    Tominey, A. F., Liese, J., Wei, S., Kowski, K., Schrader, T., & Kraft, A. (2010). RAFT polymers for protein recognition. Beilstein Journal of Organic Chemistry, 6, [66]. https://doi.org/10.3762/bjoc.6.66