RAFT polymers for protein recognition

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 copol...

Descripción completa

Detalles Bibliográficos
Autores principales: Tominey, Alan F, Liese, Julia, Wei, Sun, Kowski, Klaus, Schrader, Thomas, Kraft, Arno
Formato: Texto
Lenguaje:English
Publicado: Beilstein-Institut 2010
Materias:
Full Research Paper
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2919265/
https://www.ncbi.nlm.nih.gov/pubmed/20703378
http://dx.doi.org/10.3762/bjoc.6.66
_version_ 1782185166176780288
author Tominey, Alan F
Liese, Julia
Wei, Sun
Kowski, Klaus
Schrader, Thomas
Kraft, Arno
author_facet Tominey, Alan F
Liese, Julia
Wei, Sun
Kowski, Klaus
Schrader, Thomas
Kraft, Arno
author_sort Tominey, Alan F
collection PubMed
description 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.
format Text
id pubmed-2919265
institution National Center for Biotechnology Information
language English
publishDate 2010
publisher Beilstein-Institut
record_format MEDLINE/PubMed
spelling pubmed-29192652010-08-11 RAFT polymers for protein recognition Tominey, Alan F Liese, Julia Wei, Sun Kowski, Klaus Schrader, Thomas Kraft, Arno Beilstein J Org Chem Full Research Paper 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. Beilstein-Institut 2010-06-17 /pmc/articles/PMC2919265/ /pubmed/20703378 http://dx.doi.org/10.3762/bjoc.6.66 Text en Copyright © 2010, Tominey et al. https://creativecommons.org/licenses/by/2.0https://www.beilstein-journals.org/bjoc/termsThis is an Open Access article under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. The license is subject to the Beilstein Journal of Organic Chemistry terms and conditions: (https://www.beilstein-journals.org/bjoc/terms)
spellingShingle Full Research Paper
Tominey, Alan F
Liese, Julia
Wei, Sun
Kowski, Klaus
Schrader, Thomas
Kraft, Arno
RAFT polymers for protein recognition
title RAFT polymers for protein recognition
title_full RAFT polymers for protein recognition
title_fullStr RAFT polymers for protein recognition
title_full_unstemmed RAFT polymers for protein recognition
title_short RAFT polymers for protein recognition
title_sort raft polymers for protein recognition
topic Full Research Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2919265/
https://www.ncbi.nlm.nih.gov/pubmed/20703378
http://dx.doi.org/10.3762/bjoc.6.66
work_keys_str_mv AT tomineyalanf raftpolymersforproteinrecognition
AT liesejulia raftpolymersforproteinrecognition
AT weisun raftpolymersforproteinrecognition
AT kowskiklaus raftpolymersforproteinrecognition
AT schraderthomas raftpolymersforproteinrecognition
AT kraftarno raftpolymersforproteinrecognition

Ejemplares similares