Improved RSV preF protein vaccine quality and stability by elucidation of supercooling-induced aggregation phenomena

[Display omitted] Through a synergistic collaboration of people with varying backgrounds and expertise, the root-cause of respiratory syncytial virus prefusion (preF) protein aggregation during freezing was identified to be supercooling. This issue was addressed through a comprehensive understanding...

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Veröffentlicht in:European journal of pharmaceutics and biopharmaceutics 2024-10, Vol.203, p.114457, Article 114457
Hauptverfasser: Cui, Tao Ju, Beugeling, Max, Kaserer, Wallace, van Heugten, Anton J.P., Capelle, Martinus A.H.
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container_end_page
container_issue
container_start_page 114457
container_title European journal of pharmaceutics and biopharmaceutics
container_volume 203
creator Cui, Tao Ju
Beugeling, Max
Kaserer, Wallace
van Heugten, Anton J.P.
Capelle, Martinus A.H.
description [Display omitted] Through a synergistic collaboration of people with varying backgrounds and expertise, the root-cause of respiratory syncytial virus prefusion (preF) protein aggregation during freezing was identified to be supercooling. This issue was addressed through a comprehensive understanding of the product. Leveraging innovative and unconventional methods, apparatus, and approaches, it was effectively determined that key parameters influencing aggregation were the nucleation temperature and the duration of supercooling. Moreover, additional measurements revealed that a transition from the preF to the postfusion conformation occurs upon supercooling, which is likely caused by cold denaturation. The importance of considering freezing conditions is highlighted supporting analytical sampling and envisioning that better understanding of sample handling/freezing process can be applied to a wide range of protein-based products.
doi_str_mv 10.1016/j.ejpb.2024.114457
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subjects Aggregation
Cold denaturation
Drug Stability
Freezing
Humans
Modeling
Protein Aggregates
Protein Stability
Respiratory Syncytial Virus Vaccines - chemistry
Respiratory Syncytial Virus Vaccines - immunology
Respiratory Syncytial Virus, Human - immunology
Respiratory Syncytial Viruses - immunology
RSV protein vaccine
Stability
Supercooling
Temperature
title Improved RSV preF protein vaccine quality and stability by elucidation of supercooling-induced aggregation phenomena
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