Biocatalytic ATRP in solution and on surfaces

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

doi:10.1016/bs.mie.2019.08.014

Biocatalytic ATRP in solution and on surfaces

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

^*Corresponding author for this work

Pure And Applied Chemistry

Research output: Chapter in Book/Report/Conference proceeding › Chapter

1 Citation (Scopus)

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 language	English
Title of host publication	Methods in Enzymology
Editors	Nico Bruns, Katja Loos
Place of Publication	Cambridge, MA
Publisher	Academic Press Inc.
Chapter	10
Pages	263-290
Number of pages	28
Volume	627
ISBN (Print)	9780128170953
DOIs	https://doi.org/10.1016/bs.mie.2019.08.014
Publication status	Published - 15 Oct 2019

Publication series

Name	Methods in Enzymology
Volume	627
ISSN (Print)	0076-6879
ISSN (Electronic)	1557-7988

Funding

This work was supported by the Swiss National Science Foundation through grants Nos. PP00P2_144697, PP00P2_172927 and Ambizione program grant 179865, as well as through the Department of Pure and Applied Chemistry of the University of Strathclyde.

Keywords

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

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10.1016/bs.mie.2019.08.014

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title = "Biocatalytic ATRP in solution and on surfaces",

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.",

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AU - Divandari, Mohammad

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AU - Bruns, Nico

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AB - 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.

KW - atom transfer radical polymerization

KW - controlled radical polymerization

KW - heme proteins

KW - laccases

KW - peroxidases

KW - reversible-deactivation radical polymerization

KW - surface-initiated polymerization

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DO - 10.1016/bs.mie.2019.08.014

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BT - Methods in Enzymology

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A2 - Loos, Katja

PB - Academic Press Inc.

CY - Cambridge, MA

ER -

Biocatalytic ATRP in solution and on surfaces

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