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On the Aggregation and Nucleation Mechanism of the Monoclonal Antibody Anti-CD20 Near Liquid-Liquid Phase Separation (LLPS)
The crystallization of Anti-CD20, a full-length monoclonal antibody, has been studied in the PEG400/Na(2)SO(4)/Water system near Liquid-Liquid Phase Separation (LLPS) conditions by both sitting-drop vapour diffusion and batch methods. In order to understand the Anti-CD20 crystallization propensity i...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7264149/ https://www.ncbi.nlm.nih.gov/pubmed/32483267 http://dx.doi.org/10.1038/s41598-020-65776-6 |
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author | Pantuso, Elvira Mastropietro, Teresa F. Briuglia, Maria L. Gerard, Charline J. J. Curcio, Efrem ter Horst, Joop H. Nicoletta, Fiore P. Di Profio, Gianluca |
author_facet | Pantuso, Elvira Mastropietro, Teresa F. Briuglia, Maria L. Gerard, Charline J. J. Curcio, Efrem ter Horst, Joop H. Nicoletta, Fiore P. Di Profio, Gianluca |
author_sort | Pantuso, Elvira |
collection | PubMed |
description | The crystallization of Anti-CD20, a full-length monoclonal antibody, has been studied in the PEG400/Na(2)SO(4)/Water system near Liquid-Liquid Phase Separation (LLPS) conditions by both sitting-drop vapour diffusion and batch methods. In order to understand the Anti-CD20 crystallization propensity in the solvent system of different compositions, we investigated some measurable parameters, normally used to assess protein conformational and colloidal stability in solution, with the aim to understand the aggregation mechanism of this complex biomacromolecule. We propose that under crystallization conditions a minor population of specifically aggregated protein molecules are present. While this minor species hardly contributes to the measured average solution behaviour, it induces and promotes crystal formation. The existence of this minor species is the result of the LLPS occurring concomitantly under crystallization conditions. |
format | Online Article Text |
id | pubmed-7264149 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-72641492020-06-05 On the Aggregation and Nucleation Mechanism of the Monoclonal Antibody Anti-CD20 Near Liquid-Liquid Phase Separation (LLPS) Pantuso, Elvira Mastropietro, Teresa F. Briuglia, Maria L. Gerard, Charline J. J. Curcio, Efrem ter Horst, Joop H. Nicoletta, Fiore P. Di Profio, Gianluca Sci Rep Article The crystallization of Anti-CD20, a full-length monoclonal antibody, has been studied in the PEG400/Na(2)SO(4)/Water system near Liquid-Liquid Phase Separation (LLPS) conditions by both sitting-drop vapour diffusion and batch methods. In order to understand the Anti-CD20 crystallization propensity in the solvent system of different compositions, we investigated some measurable parameters, normally used to assess protein conformational and colloidal stability in solution, with the aim to understand the aggregation mechanism of this complex biomacromolecule. We propose that under crystallization conditions a minor population of specifically aggregated protein molecules are present. While this minor species hardly contributes to the measured average solution behaviour, it induces and promotes crystal formation. The existence of this minor species is the result of the LLPS occurring concomitantly under crystallization conditions. Nature Publishing Group UK 2020-06-01 /pmc/articles/PMC7264149/ /pubmed/32483267 http://dx.doi.org/10.1038/s41598-020-65776-6 Text en © The Author(s) 2020 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Article Pantuso, Elvira Mastropietro, Teresa F. Briuglia, Maria L. Gerard, Charline J. J. Curcio, Efrem ter Horst, Joop H. Nicoletta, Fiore P. Di Profio, Gianluca On the Aggregation and Nucleation Mechanism of the Monoclonal Antibody Anti-CD20 Near Liquid-Liquid Phase Separation (LLPS) |
title | On the Aggregation and Nucleation Mechanism of the Monoclonal Antibody Anti-CD20 Near Liquid-Liquid Phase Separation (LLPS) |
title_full | On the Aggregation and Nucleation Mechanism of the Monoclonal Antibody Anti-CD20 Near Liquid-Liquid Phase Separation (LLPS) |
title_fullStr | On the Aggregation and Nucleation Mechanism of the Monoclonal Antibody Anti-CD20 Near Liquid-Liquid Phase Separation (LLPS) |
title_full_unstemmed | On the Aggregation and Nucleation Mechanism of the Monoclonal Antibody Anti-CD20 Near Liquid-Liquid Phase Separation (LLPS) |
title_short | On the Aggregation and Nucleation Mechanism of the Monoclonal Antibody Anti-CD20 Near Liquid-Liquid Phase Separation (LLPS) |
title_sort | on the aggregation and nucleation mechanism of the monoclonal antibody anti-cd20 near liquid-liquid phase separation (llps) |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7264149/ https://www.ncbi.nlm.nih.gov/pubmed/32483267 http://dx.doi.org/10.1038/s41598-020-65776-6 |
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