ArticleMolecular pharmaceutics2012
Localized hydration in lyophilized myoglobin by hydrogen-deuterium exchange mass spectrometry. 2. Exchange kinetics.
Article in Molecular pharmaceutics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 43 citations in OpenAlex.
- Understanding dry proteins and their protection with solid-state hydrogen-deuterium exchange.Protein science : a publication of the Protein Society · 2025Review
- Application of SPRA Technology for Delivery of Erythropoietin: Stability Evaluation of Conjugated Erythropoietin with Adamantane and in SPRA Inclusion Complex.Iranian journal of pharmaceutical research : IJPR · 2022Article
- Advances in Hydrogen/Deuterium Exchange Mass Spectrometry and the Pursuit of Challenging Biological Systems.Chemical reviews · 2022Review
- Understanding the Impact of Protein-Excipient Interactions on Physical Stability of Spray-Dried Protein Solids.Molecular pharmaceutics · 2021Article
- Analytical Techniques for Structural Characterization of Proteins in Solid Pharmaceutical Forms: An Overview.Pharmaceutics · 2021Review
- Effects of Drying Process on an IgG1 Monoclonal Antibody Using Solid-State Hydrogen Deuterium Exchange with Mass Spectrometric Analysis (ssHDX-MS).Pharmaceutical research · 2018Article
- Process and Formulation Effects on Protein Structure in Lyophilized Solids Using Mass Spectrometric Methods.Journal of pharmaceutical sciences · 2016Article
- Mass spectrometric approaches to study protein structure and interactions in lyophilized powders.Journal of visualized experiments : JoVE · 2015Article
- Applications of hydrogen/deuterium exchange MS from 2012 to 2014.Analytical chemistry · 2015Review
- Characterizing Protein Structure, Dynamics and Conformation in Lyophilized Solids.Current pharmaceutical design · 2015Review
- Predicting protein aggregation during storage in lyophilized solids using solid state amide hydrogen/deuterium exchange with mass spectrometric analysis (ssHDX-MS).Molecular pharmaceutics · 2014Article
- Photolytic labeling to probe molecular interactions in lyophilized powders.Molecular pharmaceutics · 2013Article
- Localized hydration in lyophilized myoglobin by hydrogen-deuterium exchange mass spectrometry. 1. Exchange mapping.Molecular pharmaceutics · 2012Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Solid-state hydrogen-deuterium exchange with mass spectrometric analysis (ssHDX) is a promising method for characterizing proteins in amorphous solids. Though analysis of HDX kinetics is informative and well-established in solution, application of these methods to solid samples is complicated by possible heterogeneities in the solid. The studies reported here provide a detailed analysis of the kinetics of hydration and ssHDX for equine myoglobin (Mb) in solid matrices containing sucrose or mannitol. Water sorption was rapid relative to ssHDX, indicating that ssHDX kinetics was not limited by bulk water transport. Deuterium uptake in solids was well-characterized by a biexponential model; values for regression parameters provided insight into differences between the two solid matrices. Analysis of the widths of peptide mass envelopes revealed that, in solution, an apparent EX2 mechanism prevails, consistent with native conformation of the protein. In contrast, in mannitol-containing samples, a smaller non-native subpopulation exchanges by an EX1-like mechanism. Together, the results indicate that the analysis of ssHDX kinetic data and of the widths of peptide mass envelopes is useful in screening solid formulations of protein drugs for the presence of non-native species that cannot be detected by amide I FTIR.
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