Contradictory Effects of Different Freezing Rates on Visible Bubbles and Reconstitution Time during the Reconstitution of Freeze-Dried High-Concentration Monoclonal Antibody Formulations

The freezing rate is a critical factor governing ice nucleation and growth during freeze-drying, which directly determines the microvoid architecture of the freeze-dried cake and its reconstitution properties. This study systematically evaluates the effects of controlled freezing methods on reconstitution time, formation of visible bubbles (VBs), and long-term stability of high-concentration monoclonal antibody (mAb) formulations─addressing a pivotal challenge in freeze-drying process development. Solid-state microstructure was analyzed using scanning electron microscopy and mercury intrusion porosimetry. Paradoxically, accelerated freezing rates had divergent effects on reconstitution: they shortened the reconstitution time but increased the level of generation of VBs. Nonetheless, protein stability─as assessed by size exclusion chromatography and ion-exchange chromatography, remained unaffected across different freezing rates. Importantly, employing an intermediate freezing rate significantly reduced VB formation and shortened the reconstitution time for high-concentration mAb formulations. These results underscore freezing rate modulation as an essential strategy for optimizing the reconstitution performance of freeze-dried high-concentration biologics without compromising stability, offering valuable insights for industrial pharmaceutical development.

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Publication Details

Journal
Molecular Pharmaceutics
Published
2025-11-13
DOI
https://doi.org/10.1021/acs.molpharmaceut.5c01347
Primary Topic
Protein purification and stability
Type
article
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article

Contradictory Effects of Different Freezing Rates on Visible Bubbles and Reconstitution Time during the Reconstitution of Freeze-Dried High-Concentration Monoclonal Antibody Formulations

Wei‐Jie Fang, Y. Wang, Changyun Xiong, Yuhang Sun et al.
Molecular Pharmaceutics
Protein purification and stability
article

Contradictory Effects of Different Freezing Rates on Visible Bubbles and Reconstitution Time during the Reconstitution of Freeze-Dried High-Concentration Monoclonal Antibody Formulations

Wei‐Jie Fang, Y. Wang, Changyun Xiong, Yuhang Sun, Rui Xing, Zhi Ding, Han Gao, Jun Ouyang
article en

Abstract

The freezing rate is a critical factor governing ice nucleation and growth during freeze-drying, which directly determines the microvoid architecture of the freeze-dried cake and its reconstitution properties. This study systematically evaluates the effects of controlled freezing methods on reconstitution time, formation of visible bubbles (VBs), and long-term stability of high-concentration monoclonal antibody (mAb) formulations─addressing a pivotal challenge in freeze-drying process development. Solid-state microstructure was analyzed using scanning electron microscopy and mercury intrusion porosimetry. Paradoxically, accelerated freezing rates had divergent effects on reconstitution: they shortened the reconstitution time but increased the level of generation of VBs. Nonetheless, protein stability─as assessed by size exclusion chromatography and ion-exchange chromatography, remained unaffected across different freezing rates. Importantly, employing an intermediate freezing rate significantly reduced VB formation and shortened the reconstitution time for high-concentration mAb formulations. These results underscore freezing rate modulation as an essential strategy for optimizing the reconstitution performance of freeze-dried high-concentration biologics without compromising stability, offering valuable insights for industrial pharmaceutical development.

Molecular PharmaceuticsVol. 22(12)
Jungheinrich (Germany) (DE), Ningbo Science and Technology Bureau (CN), Institute of Forensic Science (CN), ZheJiang Institute For Food and Drug Control (CN), Hangzhou Medical College (CN), Zhejiang University (CN), Taizhou University (CN)
Openalex Percentile: Top 70%
Protein purification and stability
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