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Suppression of IgM Proteolysis by Conformational Stabilization Through Excipients

Protease activity from host cell lines may cause product loss or affect the quality of recombinant proteins. In this study, we showed that excipients like glycine and sorbitol reduce the proteolysis of an immunoglobulin M (IgM) in the presence of added proteases like α-chymotrypsin, papain, and peps...

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Detalles Bibliográficos
Autores principales: Mueller, Monika, Loh, Maybelle Q. T., Gagnon, Pete
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Austrian Journal of Pharmaceutical Sciences 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4727821/
https://www.ncbi.nlm.nih.gov/pubmed/26839826
http://dx.doi.org/10.3797/scipharm.1501-12
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author Mueller, Monika
Loh, Maybelle Q. T.
Gagnon, Pete
author_facet Mueller, Monika
Loh, Maybelle Q. T.
Gagnon, Pete
author_sort Mueller, Monika
collection PubMed
description Protease activity from host cell lines may cause product loss or affect the quality of recombinant proteins. In this study, we showed that excipients like glycine and sorbitol reduce the proteolysis of an immunoglobulin M (IgM) in the presence of added proteases like α-chymotrypsin, papain, and pepsin. The activity of the proteases in the IgM-protective environments was conserved or even enhanced as tested using low molecular weight substrates. Thus, a higher resistance against proteolytic degradation appears to be caused by the conformational stabilization of the IgM due to preferential exclusion of sorbitol and glycine.
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spelling pubmed-47278212016-02-02 Suppression of IgM Proteolysis by Conformational Stabilization Through Excipients Mueller, Monika Loh, Maybelle Q. T. Gagnon, Pete Sci Pharm Research Article Protease activity from host cell lines may cause product loss or affect the quality of recombinant proteins. In this study, we showed that excipients like glycine and sorbitol reduce the proteolysis of an immunoglobulin M (IgM) in the presence of added proteases like α-chymotrypsin, papain, and pepsin. The activity of the proteases in the IgM-protective environments was conserved or even enhanced as tested using low molecular weight substrates. Thus, a higher resistance against proteolytic degradation appears to be caused by the conformational stabilization of the IgM due to preferential exclusion of sorbitol and glycine. The Austrian Journal of Pharmaceutical Sciences 2015 2015-03-04 /pmc/articles/PMC4727821/ /pubmed/26839826 http://dx.doi.org/10.3797/scipharm.1501-12 Text en Copyright: © Mueller et al. http://creativecommons.org/licenses/by/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Mueller, Monika
Loh, Maybelle Q. T.
Gagnon, Pete
Suppression of IgM Proteolysis by Conformational Stabilization Through Excipients
title Suppression of IgM Proteolysis by Conformational Stabilization Through Excipients
title_full Suppression of IgM Proteolysis by Conformational Stabilization Through Excipients
title_fullStr Suppression of IgM Proteolysis by Conformational Stabilization Through Excipients
title_full_unstemmed Suppression of IgM Proteolysis by Conformational Stabilization Through Excipients
title_short Suppression of IgM Proteolysis by Conformational Stabilization Through Excipients
title_sort suppression of igm proteolysis by conformational stabilization through excipients
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4727821/
https://www.ncbi.nlm.nih.gov/pubmed/26839826
http://dx.doi.org/10.3797/scipharm.1501-12
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