An open-source automated PEG precipitation assay to measure the relative solubility of proteins with low material requirement
Abstract The solubility of proteins correlates with a variety of their properties, including function, production yield, pharmacokinetics, and formulation at high concentrations. High solubility is therefore a key requirement for the development of protein-based reagents for applications in life sci...
Guardado en:
Autores principales: | , , |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2021
|
Materias: | |
Acceso en línea: | https://doaj.org/article/b5f7828ff8824c158a7da76797f5c5ae |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
id |
oai:doaj.org-article:b5f7828ff8824c158a7da76797f5c5ae |
---|---|
record_format |
dspace |
spelling |
oai:doaj.org-article:b5f7828ff8824c158a7da76797f5c5ae2021-11-14T12:22:30ZAn open-source automated PEG precipitation assay to measure the relative solubility of proteins with low material requirement10.1038/s41598-021-01126-42045-2322https://doaj.org/article/b5f7828ff8824c158a7da76797f5c5ae2021-11-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-01126-4https://doaj.org/toc/2045-2322Abstract The solubility of proteins correlates with a variety of their properties, including function, production yield, pharmacokinetics, and formulation at high concentrations. High solubility is therefore a key requirement for the development of protein-based reagents for applications in life sciences, biotechnology, diagnostics, and therapeutics. Accurate solubility measurements, however, remain challenging and resource intensive, which limits their throughput and hence their applicability at the early stages of development pipelines, when long-lists of candidates are typically available in minute amounts. Here, we present an automated method based on the titration of a crowding agent (polyethylene glycol, PEG) to quantitatively assess relative solubility of proteins using about 200 µg of purified material. Our results demonstrate that this method is accurate and economical in material requirement and costs of reagents, which makes it suitable for high-throughput screening. This approach is freely-shared and based on a low cost, open-source liquid-handling robot. We anticipate that this method will facilitate the assessment of the developability of proteins and make it substantially more accessible.Marc OellerPietro SormanniMichele VendruscoloNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-10 (2021) |
institution |
DOAJ |
collection |
DOAJ |
language |
EN |
topic |
Medicine R Science Q |
spellingShingle |
Medicine R Science Q Marc Oeller Pietro Sormanni Michele Vendruscolo An open-source automated PEG precipitation assay to measure the relative solubility of proteins with low material requirement |
description |
Abstract The solubility of proteins correlates with a variety of their properties, including function, production yield, pharmacokinetics, and formulation at high concentrations. High solubility is therefore a key requirement for the development of protein-based reagents for applications in life sciences, biotechnology, diagnostics, and therapeutics. Accurate solubility measurements, however, remain challenging and resource intensive, which limits their throughput and hence their applicability at the early stages of development pipelines, when long-lists of candidates are typically available in minute amounts. Here, we present an automated method based on the titration of a crowding agent (polyethylene glycol, PEG) to quantitatively assess relative solubility of proteins using about 200 µg of purified material. Our results demonstrate that this method is accurate and economical in material requirement and costs of reagents, which makes it suitable for high-throughput screening. This approach is freely-shared and based on a low cost, open-source liquid-handling robot. We anticipate that this method will facilitate the assessment of the developability of proteins and make it substantially more accessible. |
format |
article |
author |
Marc Oeller Pietro Sormanni Michele Vendruscolo |
author_facet |
Marc Oeller Pietro Sormanni Michele Vendruscolo |
author_sort |
Marc Oeller |
title |
An open-source automated PEG precipitation assay to measure the relative solubility of proteins with low material requirement |
title_short |
An open-source automated PEG precipitation assay to measure the relative solubility of proteins with low material requirement |
title_full |
An open-source automated PEG precipitation assay to measure the relative solubility of proteins with low material requirement |
title_fullStr |
An open-source automated PEG precipitation assay to measure the relative solubility of proteins with low material requirement |
title_full_unstemmed |
An open-source automated PEG precipitation assay to measure the relative solubility of proteins with low material requirement |
title_sort |
open-source automated peg precipitation assay to measure the relative solubility of proteins with low material requirement |
publisher |
Nature Portfolio |
publishDate |
2021 |
url |
https://doaj.org/article/b5f7828ff8824c158a7da76797f5c5ae |
work_keys_str_mv |
AT marcoeller anopensourceautomatedpegprecipitationassaytomeasuretherelativesolubilityofproteinswithlowmaterialrequirement AT pietrosormanni anopensourceautomatedpegprecipitationassaytomeasuretherelativesolubilityofproteinswithlowmaterialrequirement AT michelevendruscolo anopensourceautomatedpegprecipitationassaytomeasuretherelativesolubilityofproteinswithlowmaterialrequirement AT marcoeller opensourceautomatedpegprecipitationassaytomeasuretherelativesolubilityofproteinswithlowmaterialrequirement AT pietrosormanni opensourceautomatedpegprecipitationassaytomeasuretherelativesolubilityofproteinswithlowmaterialrequirement AT michelevendruscolo opensourceautomatedpegprecipitationassaytomeasuretherelativesolubilityofproteinswithlowmaterialrequirement |
_version_ |
1718429251895558144 |