ArticleJournal of pharmaceutical sciences2016
Process and Formulation Effects on Protein Structure in Lyophilized Solids Using Mass Spectrometric Methods.
Article in Journal of pharmaceutical sciences, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed.
- Electrostatic spray drying for monoclonal antibody formulation.International journal of pharmaceutics · 2021Article
- Pharmaceutical protein solids: Drying technology, solid-state characterization and stability.Advanced drug delivery reviews · 2021Review
- Effects of drying method and excipient on the structure and physical stability of protein solids: Freeze drying vs. spray freeze drying.International journal of pharmaceutics · 2021Article
- Effects of drying method and excipient on structure and stability of protein solids using solid-state hydrogen/deuterium exchange mass spectrometry (ssHDX-MS).International journal of pharmaceutics · 2019Article
- Effects of Drying Process on an IgG1 Monoclonal Antibody Using Solid-State Hydrogen Deuterium Exchange with Mass Spectrometric Analysis (ssHDX-MS).Pharmaceutical research · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
Myoglobin (Mb) was lyophilized in the absence (Mb-A) and presence (Mb-B) of sucrose in a pilot-scale lyophilizer with or without controlled ice nucleation. Cake morphology was characterized using scanning electron microscopy, and changes in protein structure were monitored using solid-state Fourier-transform infrared spectroscopy, solid-state hydrogen-deuterium exchange-mass spectrometry, and solid-state photolytic labeling-mass spectrometry (ssPL-MS). The results showed greater variability in nucleation temperature and irregular cake structure for formulations lyophilized without controlled nucleation. Controlled nucleation resulted in nucleation at ∼(-5°C) and uniform cake structure. Formulations containing sucrose showed better retention of protein structure by all measures than formulations without sucrose. Samples lyophilized with and without controlled nucleation were similar by most measures of protein structure. However, ssPL-MS showed the greatest photoleucine incorporation and more labeled regions for Mb-B lyophilized with controlled nucleation. The data support the use of solid-state hydrogen-deuterium exchange-mass spectrometry and ssPL-MS to study formulation and process-induced conformational changes in lyophilized proteins.
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Registered trials
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