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The influence of excipients on the viscosity of monoclonal antibody solutions

The aggregation propensity of monoclonal antibodies can be modified by adding different cosolutes into the solution. A simple coarse-grained model in the combination with the thermodynamic perturbation theory was used to predict cluster distribution and viscosity of the solutions of IgG4 monoclonal...

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Autor principal: Hribar-Lee, Barbara
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10121187/
https://www.ncbi.nlm.nih.gov/pubmed/37089876
http://dx.doi.org/10.1016/j.molliq.2022.120349
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author Hribar-Lee, Barbara
author_facet Hribar-Lee, Barbara
author_sort Hribar-Lee, Barbara
collection PubMed
description The aggregation propensity of monoclonal antibodies can be modified by adding different cosolutes into the solution. A simple coarse-grained model in the combination with the thermodynamic perturbation theory was used to predict cluster distribution and viscosity of the solutions of IgG4 monoclonal anibody in the presence of L-Arginine Hydrochloride. The data were analysed using binding polynomial to describe the binding of cosolute (Arginine) to the antibody molecule. The results show that by binding to the antibody molecule the cosolute occupies some of the binding sites of the antibody, and in this way reduces the amount of binding sites available to other antibody molecules. The aggregation propensity of the antibody molecules is therefore reduced.
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spelling pubmed-101211872023-04-21 The influence of excipients on the viscosity of monoclonal antibody solutions Hribar-Lee, Barbara J Mol Liq Article The aggregation propensity of monoclonal antibodies can be modified by adding different cosolutes into the solution. A simple coarse-grained model in the combination with the thermodynamic perturbation theory was used to predict cluster distribution and viscosity of the solutions of IgG4 monoclonal anibody in the presence of L-Arginine Hydrochloride. The data were analysed using binding polynomial to describe the binding of cosolute (Arginine) to the antibody molecule. The results show that by binding to the antibody molecule the cosolute occupies some of the binding sites of the antibody, and in this way reduces the amount of binding sites available to other antibody molecules. The aggregation propensity of the antibody molecules is therefore reduced. 2022-11-15 2022-09-14 /pmc/articles/PMC10121187/ /pubmed/37089876 http://dx.doi.org/10.1016/j.molliq.2022.120349 Text en https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/ (https://creativecommons.org/licenses/by-nc-nd/4.0/) ).
spellingShingle Article
Hribar-Lee, Barbara
The influence of excipients on the viscosity of monoclonal antibody solutions
title The influence of excipients on the viscosity of monoclonal antibody solutions
title_full The influence of excipients on the viscosity of monoclonal antibody solutions
title_fullStr The influence of excipients on the viscosity of monoclonal antibody solutions
title_full_unstemmed The influence of excipients on the viscosity of monoclonal antibody solutions
title_short The influence of excipients on the viscosity of monoclonal antibody solutions
title_sort influence of excipients on the viscosity of monoclonal antibody solutions
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10121187/
https://www.ncbi.nlm.nih.gov/pubmed/37089876
http://dx.doi.org/10.1016/j.molliq.2022.120349
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