ArticleJournal of pharmaceutical sciences2014
Freezing-induced perturbation of tertiary structure of a monoclonal antibody.
Article in Journal of pharmaceutical sciences, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Managing Dissolved Air Throughout Freeze-Thaw Process to Reduce Aggregation of Human Serum Albumin.AAPS PharmSciTech · 2026Article
- Effect of a smart temperature logger on correctly storing biological disease-modifying antirheumatic drugs at home: a pre-post study.European journal of hospital pharmacy : science and practice · 2025Article
- Incorporating Cryopreservation Evaluations Into the Design of Cell-Based Drug Delivery Systems: An Opinion Paper.Frontiers in immunology · 2022Article
- The effect of temperature on the stability of PCSK-9 monoclonal antibody: an experimental study.Lipids in health and disease · 2021Article
- Investigation of the reversibility of freeze/thaw stress-induced protein instability using heat cycling as a function of different cryoprotectants.Bioprocess and biosystems engineering · 2020Article
- Characterizing and Minimizing Aggregation and Particle Formation of Three Recombinant Fusion-Protein Bulk Antigens for Use in a Candidate Trivalent Rotavirus Vaccine.Journal of pharmaceutical sciences · 2020Article
- Impact of Buffer, Protein Concentration and Sucrose Addition on the Aggregation and Particle Formation during Freezing and Thawing.Pharmaceutical research · 2018Article
- The Impact of Inadequate Temperature Storage Conditions on Aggregate and Particle Formation in Drugs Containing Tumor Necrosis Factor-Alpha Inhibitors.Pharmaceutical research · 2018Article
- Molecular and functional analysis of monoclonal antibodies in support of biologics development.Protein & cell · 2018Review
- Engineering the surface properties of a human monoclonal antibody prevents self-association and rapid clearance in vivo.Scientific reports · 2016Article
- Characterization of mAb dimers reveals predominant dimer forms common in therapeutic mAbs.mAbs · 2016Article
- Protein freeze concentration and micro-segregation analysed in a temperature-controlled freeze container.Biotechnology reports (Amsterdam, Netherlands) · 2015Article
- Physical characterization and in vitro biological impact of highly aggregated antibodies separated into size-enriched populations by fluorescence-activated cell sorting.Journal of pharmaceutical sciences · 2015Article
- Review
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Authors and funding
5 authors.
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Abstract
We studied the effects of pH and solution additives on freezing-induced perturbations in the tertiary structure of a monoclonal antibody (mAb) by intrinsic tryptophan fluorescence spectroscopy. In general, freezing caused perturbations in the tertiary structure of the mAb, which were reversible or irreversible depending on the pH or excipients present in the formulation. Protein aggregation occurred in freeze-thawed samples in which perturbations of the tertiary structure were observed, but the levels of protein aggregates formed were not proportional to the degree of structural perturbation. Protein aggregation also occurred in freeze-thawed samples without obvious structural perturbations, most likely because of freeze concentration of protein and salts, and thus reduced protein colloidal stability. Therefore, freezing-induced protein aggregation may or may not first involve the perturbation of its native structure, followed by the assembly processes to form aggregates. Depending on the solution conditions, either step can be rate limiting. Finally, this study demonstrates the potential of fluorescence spectroscopy as a valuable tool for screening therapeutic protein formulations subjected to freeze-thaw stress.
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