The impact of variation in freezing and thawing process parameters on the critical quality attributes of a monoclonal antibody

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dc.contributor.advisor Crean, Abina en
dc.contributor.advisor Vucen, Sonja en
dc.contributor.author Day, Neil
dc.date.accessioned 2020-05-18T09:38:15Z
dc.date.available 2020-05-18T09:38:15Z
dc.date.issued 2019-09-23
dc.date.submitted 2019-09-23
dc.identifier.citation Day, N. B. 2019. The impact of variation in freezing and thawing process parameters on the critical quality attributes of a monoclonal antibody. MRes Thesis, University College Cork. en
dc.identifier.endpage 105 en
dc.identifier.uri http://hdl.handle.net/10468/9969
dc.description.abstract Therapeutic proteins or biopharmaceuticals have been playing an ever-increasing role in the treatment of human diseases over last 40 years. One of the main challenges with manufacture of these proteins is the stabilization of both the finished product and its processing intermediates during storage. Freezing and frozen storage is widely applied to improve stability of the bulk drug substance. The process of freezing a protein results in stresses that can cause protein degradation and subsequent aggregation. The aim of this project was to evaluate the effect of parameters involved with freezing and thawing of a formulated monoclonal antibody solution in polycarbonate bottles and to assess the scalability of these experiments to the respective full-scale commercial process. Initial experiments were performed to characterise the formulation and develop analytical methods that can detect change in unfolding and aggregation of a fully human IgG1 monoclonal antibody (‘Protein Y’). A designed set of experiments were then executed to understand the effect of parameters involved in freezing and thawing steps of a formulated therapeutic protein solution on protein aggregation and perturbations in tertiary structure. Results showed that the processing parameters studied caused significant variation in freeze and thaw process times, with the factors causing slower rates of freeze and thaw also shown to cause changes in the tertiary structure of Protein Y. Despite the observed changes in tertiary structure, the effect on aggregation was less pronounced, with only a significant change noted for the polydispersity index (PdI), as measured by dynamic light scattering (DLS). en
dc.format.mimetype application/pdf en
dc.language.iso en en
dc.publisher University College Cork en
dc.rights © 2019, Neil Day. en
dc.rights.uri https://creativecommons.org/licenses/by-nc-nd/4.0/ en
dc.subject Monoclonal antibody en
dc.subject Plank equation en
dc.subject Cryo-concentration en
dc.subject Freezing en
dc.subject Thawing en
dc.title The impact of variation in freezing and thawing process parameters on the critical quality attributes of a monoclonal antibody en
dc.type Masters thesis (Research) en
dc.type.qualificationlevel Masters en
dc.type.qualificationname MRes - Master of Research en
dc.internal.availability Full text available en
dc.description.version Accepted Version en
dc.description.status Not peer reviewed en
dc.internal.school Pharmacy en
dc.internal.conferring Summer 2020 en
dc.availability.bitstream openaccess


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© 2019, Neil Day. Except where otherwise noted, this item's license is described as © 2019, Neil Day.
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