Literature DB >> 35083639

Characterization of Grinding-Induced Subvisible Particles and Free Radicals in a Freeze-Dried Monoclonal Antibody Formulation.

Zhen-Yi Jing1,2, Guo-Li Huo1,2, Min-Fei Sun1,2, Bin-Bin Shen1,2, Wei-Jie Fang3,4.   

Abstract

PURPOSES: The primary objectives of this study were to investigate the degradation mechanisms of freeze-dried monoclonal antibody (mAb) formulations under mechanical grinding, assess the sensitivity and suitability of various particle analysis techniques, analyze the structure of the collected subvisible particles (SbVPs), and analyze the antioxidant mechanism of methionine (Met) under degradation process to gain a thorough understanding of the phenomenon.
METHODS: The freeze-dried mAb-X formulations underwent grinding, and the resultant SbVPs were characterized through visual inspection, flow imaging microscopy, dynamic light scattering, ultraviolet-visible spectroscopy, and size-exclusion high-performance liquid chromatography. We further evaluated the effect of different temperatures and the free radical scavenger Met on SbVP formation. The produced free radicals were detected using electron paramagnetic resonance, and Met S-oxide formation was detected using liquid chromatography-mass spectrometry. In addition, we analyzed the obtained SbVPs using capillary electrophoresis sodium dodecyl sulfate and Fourier transform infrared spectroscopy.
RESULTS: Grinding leads to SbVP formation under high temperature and free radical formation. Free radicals produced during grinding require the participation of a macromolecule. Met could then bind to the produced free radicals, thus partially protecting mAb-X from degradation while itself undergoing oxidation to form Met(O). Sensitivity differences between different particle analysis techniques were evaluated, and the obtained SbVPs showed significant changes in secondary structure and the formation of covalent aggregates and fragments.
CONCLUSIONS: Met plays the role of an antioxidant in protecting macromolecules by quenching the free radicals produced during grinding. To thoroughly characterize SbVPs, multiple and orthogonal particle analysis techniques should be used, and if necessary, SbVPs should be processed by enrichment to accurately analyze primary and high order structures.
© 2022. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.

Entities:  

Keywords:  Met(O); aggregation; flow imaging microscopy; free radical; grinding; monoclonal antibody; protein subvisible particles

Mesh:

Substances:

Year:  2022        PMID: 35083639     DOI: 10.1007/s11095-022-03170-9

Source DB:  PubMed          Journal:  Pharm Res        ISSN: 0724-8741            Impact factor:   4.200


  47 in total

1.  Shaken, not stirred: mechanical stress testing of an IgG1 antibody.

Authors:  Sylvia Kiese; Astrid Papppenberger; Wolfgang Friess; Hanns-Christian Mahler
Journal:  J Pharm Sci       Date:  2008-10       Impact factor: 3.534

Review 2.  A review of Formulations of Commercially Available Antibodies.

Authors:  Robert G Strickley; William J Lambert
Journal:  J Pharm Sci       Date:  2021-03-28       Impact factor: 3.534

3.  IgG particle formation during filling pump operation: a case study of heterogeneous nucleation on stainless steel nanoparticles.

Authors:  Anil K Tyagi; Theodore W Randolph; Aichun Dong; Kevin M Maloney; Carl Hitscherich; John F Carpenter
Journal:  J Pharm Sci       Date:  2009-01       Impact factor: 3.534

4.  Structural characterization of IgG1 mAb aggregates and particles generated under various stress conditions.

Authors:  Srivalli N Telikepalli; Ozan S Kumru; Cavan Kalonia; Reza Esfandiary; Sangeeta B Joshi; C Russell Middaugh; David B Volkin
Journal:  J Pharm Sci       Date:  2014-01-22       Impact factor: 3.534

5.  Characterization of subvisible particle formation during the filling pump operation of a monoclonal antibody solution.

Authors:  Arpan Nayak; James Colandene; Victor Bradford; Melissa Perkins
Journal:  J Pharm Sci       Date:  2011-06-22       Impact factor: 3.534

6.  Processing Impact on Monoclonal Antibody Drug Products: Protein Subvisible Particulate Formation Induced by Grinding Stress.

Authors:  Benson Gikanga; Devon Roshan Eisner; Robert Ovadia; Eric S Day; Oliver B Stauch; Yuh-Fun Maa
Journal:  PDA J Pharm Sci Technol       Date:  2016-10-27

Review 7.  Stress Factors in mAb Drug Substance Production Processes: Critical Assessment of Impact on Product Quality and Control Strategy.

Authors:  Tapan K Das; Linda O Narhi; Alavattam Sreedhara; Tim Menzen; Christoph Grapentin; Danny K Chou; Valentyn Antochshuk; Vasco Filipe
Journal:  J Pharm Sci       Date:  2019-10-05       Impact factor: 3.534

8.  Mechanically-induced aggregation of the monoclonal antibody cetuximab.

Authors:  A Lahlou; B Blanchet; M Carvalho; M Paul; A Astier
Journal:  Ann Pharm Fr       Date:  2009-07-28

9.  Shocking Data on Parcel Shipments of Protein Solutions.

Authors:  Christine Siska; Paul Harber; Bruce A Kerwin
Journal:  J Pharm Sci       Date:  2019-11-02       Impact factor: 3.534

Review 10.  Protein aggregation and immunogenicity of biotherapeutics.

Authors:  Ngoc B Pham; Wilson S Meng
Journal:  Int J Pharm       Date:  2020-06-09       Impact factor: 5.875

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