ArticleMolecular pharmaceutics2012
Localized hydration in lyophilized myoglobin by hydrogen-deuterium exchange mass spectrometry. 1. Exchange mapping.
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 21 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
21 citing papers in PubMed, 35 citations in OpenAlex.
- Investigation of the Solid-State Interactions in Lyophilized Human G-CSF Using Hydrogen-Deuterium Exchange Mass Spectrometry.Molecular pharmaceutics · 2024Article
- How Sugars Protect Dry Protein Structure.Biochemistry · 2023Article
- Article
- Calorimetric Investigation of the Relaxation Phenomena in Amorphous Lyophilized Solids.Pharmaceutics · 2021Review
- Electrostatic spray drying for monoclonal antibody formulation.International journal of pharmaceutics · 2021Article
- Analytical Techniques for Structural Characterization of Proteins in Solid Pharmaceutical Forms: An Overview.Pharmaceutics · 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
- Surface Composition and Formulation Heterogeneity of Protein Solids Produced by Spray Drying.Pharmaceutical research · 2019Article
- 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
- On-tissue Direct Monitoring of Global Hydrogen/Deuterium Exchange by MALDI Mass Spectrometry: Tissue Deuterium Exchange Mass Spectrometry (TDXMS).Molecular & cellular proteomics : MCP · 2016Article
- Process and Formulation Effects on Protein Structure in Lyophilized Solids Using Mass Spectrometric Methods.Journal of pharmaceutical sciences · 2016Article
- Photolytic Cross-Linking to Probe Protein-Protein and Protein-Matrix Interactions in Lyophilized Powders.Molecular pharmaceutics · 2015Article
- Mass spectrometric approaches to study protein structure and interactions in lyophilized powders.Journal of visualized experiments : JoVE · 2015Article
- Thiol-disulfide exchange in peptides derived from human growth hormone during lyophilization and storage in the solid state.Journal of pharmaceutical sciences · 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
- Protein aggregation and lyophilization: Protein structural descriptors as predictors of aggregation propensity.Computers & chemical engineering · 2013Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The local effects of hydration on myoglobin (Mb) in solid matrices containing mannitol or sucrose (1:1 w/w, protein:additive) were mapped using hydrogen-deuterium exchange with mass spectrometric analysis (HDX-MS) at 5 °C and compared to solution controls. Solid powders were exposed to D₂O(g) at controlled activity (a(w)) followed by reconstitution and analysis of the intact protein and peptides produced by pepsin digestion. HDX varied with matrix type, a(w), and position along the protein backbone. HDX was less in sucrose matrices than in mannitol matrices at all a(w) while the difference in solution was negligible. Differences in HDX in the two matrices were detectable despite similarities in their bulk water content. The extent of exchange in solids is proposed as a measure of the hydration of exchangeable amide groups, as well as protein conformation and dynamics; pepsin digestion allows these effects to be mapped with peptide-level resolution.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.