Efficient encapsulation of proteins with random copolymers
Inside cells of living organisms, aggregates rich in disordered proteins organize the local environment to promote cellular functions. These membraneless organelles are able to concentrate enzymes and biomolecules to regulate interactions via the multiple conformations and compositions of disordered...
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ftpubmed:oai:pubmedcentral.nih.gov:6042061 2023-05-15T13:52:35+02:00 Efficient encapsulation of proteins with random copolymers Nguyen, Trung Dac Qiao, Baofu Olvera de la Cruz, Monica 2018-06-26 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6042061/ http://www.ncbi.nlm.nih.gov/pubmed/29895685 https://doi.org/10.1073/pnas.1806207115 en eng National Academy of Sciences http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6042061/ http://www.ncbi.nlm.nih.gov/pubmed/29895685 http://dx.doi.org/10.1073/pnas.1806207115 Published under the PNAS license (http://www.pnas.org/site/aboutpnas/licenses.xhtml) . Physical Sciences Text 2018 ftpubmed https://doi.org/10.1073/pnas.1806207115 2018-12-30T01:07:41Z Inside cells of living organisms, aggregates rich in disordered proteins organize the local environment to promote cellular functions. These membraneless organelles are able to concentrate enzymes and biomolecules to regulate interactions via the multiple conformations and compositions of disordered proteins. The interior of these organelles seems to behave akin to organic solvents. This opens the possibility of assembling synthetic organelles using random copolymers that mimic disordered proteins to disperse and stabilize enzymatic proteins in different environments, including organic solvents. Here, we demonstrate that random copolymers with solvophobic and solvophilic groups can encapsulate numerous proteins, including Candida antarctica lipase B, subtilisin, cutinase, and pseudolysin, in basically any solvent. These aggregates are promising constituents of synthetic membraneless organelles. Text Antarc* Antarctica PubMed Central (PMC) Proceedings of the National Academy of Sciences 115 26 6578 6583 |
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Physical Sciences Nguyen, Trung Dac Qiao, Baofu Olvera de la Cruz, Monica Efficient encapsulation of proteins with random copolymers |
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Physical Sciences |
description |
Inside cells of living organisms, aggregates rich in disordered proteins organize the local environment to promote cellular functions. These membraneless organelles are able to concentrate enzymes and biomolecules to regulate interactions via the multiple conformations and compositions of disordered proteins. The interior of these organelles seems to behave akin to organic solvents. This opens the possibility of assembling synthetic organelles using random copolymers that mimic disordered proteins to disperse and stabilize enzymatic proteins in different environments, including organic solvents. Here, we demonstrate that random copolymers with solvophobic and solvophilic groups can encapsulate numerous proteins, including Candida antarctica lipase B, subtilisin, cutinase, and pseudolysin, in basically any solvent. These aggregates are promising constituents of synthetic membraneless organelles. |
format |
Text |
author |
Nguyen, Trung Dac Qiao, Baofu Olvera de la Cruz, Monica |
author_facet |
Nguyen, Trung Dac Qiao, Baofu Olvera de la Cruz, Monica |
author_sort |
Nguyen, Trung Dac |
title |
Efficient encapsulation of proteins with random copolymers |
title_short |
Efficient encapsulation of proteins with random copolymers |
title_full |
Efficient encapsulation of proteins with random copolymers |
title_fullStr |
Efficient encapsulation of proteins with random copolymers |
title_full_unstemmed |
Efficient encapsulation of proteins with random copolymers |
title_sort |
efficient encapsulation of proteins with random copolymers |
publisher |
National Academy of Sciences |
publishDate |
2018 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6042061/ http://www.ncbi.nlm.nih.gov/pubmed/29895685 https://doi.org/10.1073/pnas.1806207115 |
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Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6042061/ http://www.ncbi.nlm.nih.gov/pubmed/29895685 http://dx.doi.org/10.1073/pnas.1806207115 |
op_rights |
Published under the PNAS license (http://www.pnas.org/site/aboutpnas/licenses.xhtml) . |
op_doi |
https://doi.org/10.1073/pnas.1806207115 |
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Proceedings of the National Academy of Sciences |
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115 |
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26 |
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6578 |
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6583 |
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1766257008260939776 |