An in vivo platform to select and evolve aggregation-resistant proteins

Protein aggregation remains a significant challenge for manufacturing of protein biopharmaceuticals. Here, the authors demonstrate the use of directed evolution and an assay for in vivo innate protein aggregation-propensity to generate aggregation-resistant scFv fragments.

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Autores principales: Jessica S. Ebo, Janet C. Saunders, Paul W. A. Devine, Alice M. Gordon, Amy S. Warwick, Bob Schiffrin, Stacey E. Chin, Elizabeth England, James D. Button, Christopher Lloyd, Nicholas J. Bond, Alison E. Ashcroft, Sheena E. Radford, David C. Lowe, David J. Brockwell
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Lenguaje:EN
Publicado: Nature Portfolio 2020
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Acceso en línea:https://doaj.org/article/7cd4d27ccee2435a841e247a296e334c
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spelling oai:doaj.org-article:7cd4d27ccee2435a841e247a296e334c2021-12-02T14:40:38ZAn in vivo platform to select and evolve aggregation-resistant proteins10.1038/s41467-020-15667-12041-1723https://doaj.org/article/7cd4d27ccee2435a841e247a296e334c2020-04-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-15667-1https://doaj.org/toc/2041-1723Protein aggregation remains a significant challenge for manufacturing of protein biopharmaceuticals. Here, the authors demonstrate the use of directed evolution and an assay for in vivo innate protein aggregation-propensity to generate aggregation-resistant scFv fragments.Jessica S. EboJanet C. SaundersPaul W. A. DevineAlice M. GordonAmy S. WarwickBob SchiffrinStacey E. ChinElizabeth EnglandJames D. ButtonChristopher LloydNicholas J. BondAlison E. AshcroftSheena E. RadfordDavid C. LoweDavid J. BrockwellNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-12 (2020)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Jessica S. Ebo
Janet C. Saunders
Paul W. A. Devine
Alice M. Gordon
Amy S. Warwick
Bob Schiffrin
Stacey E. Chin
Elizabeth England
James D. Button
Christopher Lloyd
Nicholas J. Bond
Alison E. Ashcroft
Sheena E. Radford
David C. Lowe
David J. Brockwell
An in vivo platform to select and evolve aggregation-resistant proteins
description Protein aggregation remains a significant challenge for manufacturing of protein biopharmaceuticals. Here, the authors demonstrate the use of directed evolution and an assay for in vivo innate protein aggregation-propensity to generate aggregation-resistant scFv fragments.
format article
author Jessica S. Ebo
Janet C. Saunders
Paul W. A. Devine
Alice M. Gordon
Amy S. Warwick
Bob Schiffrin
Stacey E. Chin
Elizabeth England
James D. Button
Christopher Lloyd
Nicholas J. Bond
Alison E. Ashcroft
Sheena E. Radford
David C. Lowe
David J. Brockwell
author_facet Jessica S. Ebo
Janet C. Saunders
Paul W. A. Devine
Alice M. Gordon
Amy S. Warwick
Bob Schiffrin
Stacey E. Chin
Elizabeth England
James D. Button
Christopher Lloyd
Nicholas J. Bond
Alison E. Ashcroft
Sheena E. Radford
David C. Lowe
David J. Brockwell
author_sort Jessica S. Ebo
title An in vivo platform to select and evolve aggregation-resistant proteins
title_short An in vivo platform to select and evolve aggregation-resistant proteins
title_full An in vivo platform to select and evolve aggregation-resistant proteins
title_fullStr An in vivo platform to select and evolve aggregation-resistant proteins
title_full_unstemmed An in vivo platform to select and evolve aggregation-resistant proteins
title_sort in vivo platform to select and evolve aggregation-resistant proteins
publisher Nature Portfolio
publishDate 2020
url https://doaj.org/article/7cd4d27ccee2435a841e247a296e334c
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