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 |
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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 |
format | Article |
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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.</description><identifier>ISSN: 0939-6411</identifier><identifier>ISSN: 1873-3441</identifier><identifier>EISSN: 1873-3441</identifier><identifier>DOI: 10.1016/j.ejpb.2024.114457</identifier><identifier>PMID: 39151707</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>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</subject><ispartof>European journal of pharmaceutics and biopharmaceutics, 2024-10, Vol.203, p.114457, Article 114457</ispartof><rights>2024 Elsevier B.V.</rights><rights>Copyright © 2024 Elsevier B.V. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c237t-e2fce63ed48547a3c0af1fe5ccd1cf439c2ab03bc506baae2ef8f073a07ed5bc3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.ejpb.2024.114457$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/39151707$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cui, Tao Ju</creatorcontrib><creatorcontrib>Beugeling, Max</creatorcontrib><creatorcontrib>Kaserer, Wallace</creatorcontrib><creatorcontrib>van Heugten, Anton J.P.</creatorcontrib><creatorcontrib>Capelle, Martinus A.H.</creatorcontrib><title>Improved RSV preF protein vaccine quality and stability by elucidation of supercooling-induced aggregation phenomena</title><title>European journal of pharmaceutics and biopharmaceutics</title><addtitle>Eur J Pharm Biopharm</addtitle><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.</description><subject>Aggregation</subject><subject>Cold denaturation</subject><subject>Drug Stability</subject><subject>Freezing</subject><subject>Humans</subject><subject>Modeling</subject><subject>Protein Aggregates</subject><subject>Protein Stability</subject><subject>Respiratory Syncytial Virus Vaccines - chemistry</subject><subject>Respiratory Syncytial Virus Vaccines - immunology</subject><subject>Respiratory Syncytial Virus, Human - immunology</subject><subject>Respiratory Syncytial Viruses - immunology</subject><subject>RSV protein vaccine</subject><subject>Stability</subject><subject>Supercooling</subject><subject>Temperature</subject><issn>0939-6411</issn><issn>1873-3441</issn><issn>1873-3441</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2024</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kMFq3DAQhkVpaTZpXyCHomMv3kiWvFpDLyU0TSAQaJtchTwabbTYkiPZC_v21dZpj73MMPD9P8xHyCVna8745mq_xv3YrWtWyzXnUjbqDVnxrRKVkJK_JSvWirbaSM7PyHnOe8aYVM32PTkTLW-4YmpFprthTPGAlv74-UTHhDdlxAl9oAcD4APSl9n0fjpSEyzNk-n8n6s7Uuxn8NZMPgYaHc3ziAli7H3YVT7YGUqr2e0S7hZmfMYQBwzmA3nnTJ_x4-u-II83335d31b3D9_vrr_eV1ALNVVYO8CNQCu3jVRGADOOO2wALAcnRQu16ZjooGGbzhis0W0dU8IwhbbpQFyQz0tveellxjzpwWfAvjcB45y1YK1kRZUSBa0XFFLMOaHTY_KDSUfNmT7Z1nt9sq1PtvViu4Q-vfbP3YD2X-Sv3gJ8WQAsXx48Jp3BYyhifEKYtI3-f_2_AbgalEI</recordid><startdate>202410</startdate><enddate>202410</enddate><creator>Cui, Tao Ju</creator><creator>Beugeling, Max</creator><creator>Kaserer, Wallace</creator><creator>van Heugten, Anton J.P.</creator><creator>Capelle, Martinus A.H.</creator><general>Elsevier B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>202410</creationdate><title>Improved RSV preF protein vaccine quality and stability by elucidation of supercooling-induced aggregation phenomena</title><author>Cui, Tao Ju ; Beugeling, Max ; Kaserer, Wallace ; van Heugten, Anton J.P. ; Capelle, Martinus A.H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c237t-e2fce63ed48547a3c0af1fe5ccd1cf439c2ab03bc506baae2ef8f073a07ed5bc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2024</creationdate><topic>Aggregation</topic><topic>Cold denaturation</topic><topic>Drug Stability</topic><topic>Freezing</topic><topic>Humans</topic><topic>Modeling</topic><topic>Protein Aggregates</topic><topic>Protein Stability</topic><topic>Respiratory Syncytial Virus Vaccines - chemistry</topic><topic>Respiratory Syncytial Virus Vaccines - immunology</topic><topic>Respiratory Syncytial Virus, Human - immunology</topic><topic>Respiratory Syncytial Viruses - immunology</topic><topic>RSV protein vaccine</topic><topic>Stability</topic><topic>Supercooling</topic><topic>Temperature</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cui, Tao Ju</creatorcontrib><creatorcontrib>Beugeling, Max</creatorcontrib><creatorcontrib>Kaserer, Wallace</creatorcontrib><creatorcontrib>van Heugten, Anton J.P.</creatorcontrib><creatorcontrib>Capelle, Martinus A.H.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>European journal of pharmaceutics and biopharmaceutics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cui, Tao Ju</au><au>Beugeling, Max</au><au>Kaserer, Wallace</au><au>van Heugten, Anton J.P.</au><au>Capelle, Martinus A.H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Improved RSV preF protein vaccine quality and stability by elucidation of supercooling-induced aggregation phenomena</atitle><jtitle>European journal of pharmaceutics and biopharmaceutics</jtitle><addtitle>Eur J Pharm Biopharm</addtitle><date>2024-10</date><risdate>2024</risdate><volume>203</volume><spage>114457</spage><pages>114457-</pages><artnum>114457</artnum><issn>0939-6411</issn><issn>1873-3441</issn><eissn>1873-3441</eissn><abstract>[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.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>39151707</pmid><doi>10.1016/j.ejpb.2024.114457</doi></addata></record> |
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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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