Biocatalytic ATRP in solution and on surfaces

Kyle J. Rodriguez, Michela M. Pellizzoni, Mohammad Divandari, Edmondo M. Benetti, Nico Bruns

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

The promiscuity of enzymes allows for their implementation as catalysts for non-native chemical transformations. Utilizing the redox activity of metalloenzymes under activator regenerated by electron transfer (ARGET) ATRP conditions, well-controlled and defined polymers can be generated. In this chapter, we review bioATRP in solution and on surfaces and provide experimental protocols for hemoglobin-catalyzed ATRP and for surface-initiated biocatalytic ATRP. This chapter highlights the polymerization of acrylate and acrylamide monomers and provides detailed experimental protocols for the characterization of the polymers and of the polymer brushes.

Original languageEnglish
Title of host publicationMethods in Enzymology
EditorsNico Bruns, Katja Loos
Place of PublicationCambridge, MA
PublisherAcademic Press Inc.
Chapter10
Pages263-290
Number of pages28
Volume627
ISBN (Print)9780128170953
DOIs
Publication statusPublished - 15 Oct 2019

Publication series

NameMethods in Enzymology
Volume627
ISSN (Print)0076-6879
ISSN (Electronic)1557-7988

Keywords

  • atom transfer radical polymerization
  • controlled radical polymerization
  • heme proteins
  • laccases
  • peroxidases
  • reversible-deactivation radical polymerization
  • surface-initiated polymerization

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  • Cite this

    Rodriguez, K. J., Pellizzoni, M. M., Divandari, M., Benetti, E. M., & Bruns, N. (2019). Biocatalytic ATRP in solution and on surfaces. In N. Bruns, & K. Loos (Eds.), Methods in Enzymology (Vol. 627, pp. 263-290). (Methods in Enzymology; Vol. 627). Cambridge, MA: Academic Press Inc.. https://doi.org/10.1016/bs.mie.2019.08.014