ATRPases: using nature's catalysts in atom transfer radical polymerizations

Gergely Kali, Tilana B. Silva, Severin J. Sigg, Farzad Seidi, Kasper Renggli, Nico Bruns

Research output: Chapter in Book/Report/Conference proceedingChapter (peer-reviewed)

7 Citations (Scopus)

Abstract

Enzymes are environmentally friendly, non-toxic catalysts that have found many applications in synthetic polymer chemistry. However, until very recently no examples of enzyme-catalyzed, controlled radical polymerizations were known. Here we review the nascent field of biocatalytic atom transfer radical polymerization (ATRP). The heme proteins horseradish peroxidase, hemoglobin and catalase, as well as the copper-containing enzyme laccase have been reported to display catalytic activity in activators regenerated by electron transfer (ARGET) ATRP of two model monomers, N-isopropylacrylamide and poly(ethylene glycol) methyl ether acrylate. Bromine-terminated polymers, low polydispersity indices, linear increase in molecular weight with conversion as well as first-order kinetics indicate ATRP-type mechanisms. However, the first examples of biocatalytic ATRP also show that enzymes are much more complex catalysts than conventional ones.

Original languageEnglish
Title of host publicationProgress in Controlled Radical Polymerization
Subtitle of host publicationMechanisms and Techniques
PublisherAmerican Chemical Society
Pages171-181
Number of pages11
ISBN (Print)9780841226999
DOIs
Publication statusPublished - 1 Jan 2012

Publication series

NameACS Symposium Series
Volume1100
ISSN (Print)0097-6156
ISSN (Electronic)1947-5918

Fingerprint

Atom transfer radical polymerization
Enzymes
Catalysts
Polymers
Hemeproteins
Methyl Ethers
Bromine
Laccase
Hemoglobin
Polydispersity
Horseradish Peroxidase
Free radical polymerization
Catalase
Polyethylene glycols
Copper
Ethers
Catalyst activity
Hemoglobins
Monomers
Molecular weight

Keywords

  • enzymatic polymerization
  • acrylic monomers
  • enzymes
  • free radical polymerization
  • polydispersity
  • polyethylene glycols
  • polymers
  • atom transfer radical polymerization

Cite this

Kali, G., Silva, T. B., Sigg, S. J., Seidi, F., Renggli, K., & Bruns, N. (2012). ATRPases: using nature's catalysts in atom transfer radical polymerizations. In Progress in Controlled Radical Polymerization: Mechanisms and Techniques (pp. 171-181). (ACS Symposium Series; Vol. 1100). American Chemical Society. https://doi.org/10.1021/bk-2012-1100.ch011
Kali, Gergely ; Silva, Tilana B. ; Sigg, Severin J. ; Seidi, Farzad ; Renggli, Kasper ; Bruns, Nico. / ATRPases : using nature's catalysts in atom transfer radical polymerizations. Progress in Controlled Radical Polymerization: Mechanisms and Techniques. American Chemical Society, 2012. pp. 171-181 (ACS Symposium Series).
@inbook{1f149f78643349cdbc6677941a929097,
title = "ATRPases: using nature's catalysts in atom transfer radical polymerizations",
abstract = "Enzymes are environmentally friendly, non-toxic catalysts that have found many applications in synthetic polymer chemistry. However, until very recently no examples of enzyme-catalyzed, controlled radical polymerizations were known. Here we review the nascent field of biocatalytic atom transfer radical polymerization (ATRP). The heme proteins horseradish peroxidase, hemoglobin and catalase, as well as the copper-containing enzyme laccase have been reported to display catalytic activity in activators regenerated by electron transfer (ARGET) ATRP of two model monomers, N-isopropylacrylamide and poly(ethylene glycol) methyl ether acrylate. Bromine-terminated polymers, low polydispersity indices, linear increase in molecular weight with conversion as well as first-order kinetics indicate ATRP-type mechanisms. However, the first examples of biocatalytic ATRP also show that enzymes are much more complex catalysts than conventional ones.",
keywords = "enzymatic polymerization, acrylic monomers, enzymes, free radical polymerization, polydispersity, polyethylene glycols, polymers, atom transfer radical polymerization",
author = "Gergely Kali and Silva, {Tilana B.} and Sigg, {Severin J.} and Farzad Seidi and Kasper Renggli and Nico Bruns",
year = "2012",
month = "1",
day = "1",
doi = "10.1021/bk-2012-1100.ch011",
language = "English",
isbn = "9780841226999",
series = "ACS Symposium Series",
publisher = "American Chemical Society",
pages = "171--181",
booktitle = "Progress in Controlled Radical Polymerization",
address = "United States",

}

Kali, G, Silva, TB, Sigg, SJ, Seidi, F, Renggli, K & Bruns, N 2012, ATRPases: using nature's catalysts in atom transfer radical polymerizations. in Progress in Controlled Radical Polymerization: Mechanisms and Techniques. ACS Symposium Series, vol. 1100, American Chemical Society, pp. 171-181. https://doi.org/10.1021/bk-2012-1100.ch011

ATRPases : using nature's catalysts in atom transfer radical polymerizations. / Kali, Gergely; Silva, Tilana B.; Sigg, Severin J.; Seidi, Farzad; Renggli, Kasper; Bruns, Nico.

Progress in Controlled Radical Polymerization: Mechanisms and Techniques. American Chemical Society, 2012. p. 171-181 (ACS Symposium Series; Vol. 1100).

Research output: Chapter in Book/Report/Conference proceedingChapter (peer-reviewed)

TY - CHAP

T1 - ATRPases

T2 - using nature's catalysts in atom transfer radical polymerizations

AU - Kali, Gergely

AU - Silva, Tilana B.

AU - Sigg, Severin J.

AU - Seidi, Farzad

AU - Renggli, Kasper

AU - Bruns, Nico

PY - 2012/1/1

Y1 - 2012/1/1

N2 - Enzymes are environmentally friendly, non-toxic catalysts that have found many applications in synthetic polymer chemistry. However, until very recently no examples of enzyme-catalyzed, controlled radical polymerizations were known. Here we review the nascent field of biocatalytic atom transfer radical polymerization (ATRP). The heme proteins horseradish peroxidase, hemoglobin and catalase, as well as the copper-containing enzyme laccase have been reported to display catalytic activity in activators regenerated by electron transfer (ARGET) ATRP of two model monomers, N-isopropylacrylamide and poly(ethylene glycol) methyl ether acrylate. Bromine-terminated polymers, low polydispersity indices, linear increase in molecular weight with conversion as well as first-order kinetics indicate ATRP-type mechanisms. However, the first examples of biocatalytic ATRP also show that enzymes are much more complex catalysts than conventional ones.

AB - Enzymes are environmentally friendly, non-toxic catalysts that have found many applications in synthetic polymer chemistry. However, until very recently no examples of enzyme-catalyzed, controlled radical polymerizations were known. Here we review the nascent field of biocatalytic atom transfer radical polymerization (ATRP). The heme proteins horseradish peroxidase, hemoglobin and catalase, as well as the copper-containing enzyme laccase have been reported to display catalytic activity in activators regenerated by electron transfer (ARGET) ATRP of two model monomers, N-isopropylacrylamide and poly(ethylene glycol) methyl ether acrylate. Bromine-terminated polymers, low polydispersity indices, linear increase in molecular weight with conversion as well as first-order kinetics indicate ATRP-type mechanisms. However, the first examples of biocatalytic ATRP also show that enzymes are much more complex catalysts than conventional ones.

KW - enzymatic polymerization

KW - acrylic monomers

KW - enzymes

KW - free radical polymerization

KW - polydispersity

KW - polyethylene glycols

KW - polymers

KW - atom transfer radical polymerization

UR - http://www.scopus.com/inward/record.url?scp=84905663791&partnerID=8YFLogxK

U2 - 10.1021/bk-2012-1100.ch011

DO - 10.1021/bk-2012-1100.ch011

M3 - Chapter (peer-reviewed)

AN - SCOPUS:84905663791

SN - 9780841226999

T3 - ACS Symposium Series

SP - 171

EP - 181

BT - Progress in Controlled Radical Polymerization

PB - American Chemical Society

ER -

Kali G, Silva TB, Sigg SJ, Seidi F, Renggli K, Bruns N. ATRPases: using nature's catalysts in atom transfer radical polymerizations. In Progress in Controlled Radical Polymerization: Mechanisms and Techniques. American Chemical Society. 2012. p. 171-181. (ACS Symposium Series). https://doi.org/10.1021/bk-2012-1100.ch011