ArticleMolecular pharmaceutics2014
Predicting protein aggregation during storage in lyophilized solids using solid state amide hydrogen/deuterium exchange with mass spectrometric analysis (ssHDX-MS).
Article in Molecular pharmaceutics, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 64 citations in OpenAlex.
- Understanding dry proteins and their protection with solid-state hydrogen-deuterium exchange.Protein science : a publication of the Protein Society · 2025Review
- Investigation of the Solid-State Interactions in Lyophilized Human G-CSF Using Hydrogen-Deuterium Exchange Mass Spectrometry.Molecular pharmaceutics · 2024Article
- Effect of Buffer Salts on Physical Stability of Lyophilized and Spray-Dried Protein Formulations Containing Bovine Serum Albumin and Trehalose.Pharmaceutical research · 2023Article
- Radio Frequency - Assisted Ultrasonic Spray Freeze Drying for Pharmaceutical Protein Solids.Journal of pharmaceutical sciences · 2023Article
- Advances in Hydrogen/Deuterium Exchange Mass Spectrometry and the Pursuit of Challenging Biological Systems.Chemical reviews · 2022Review
- Processing Characteristics of Freeze-Dried Pork Powder for Meat Emulsion Gel.Food science of animal resources · 2021Article
- Water's Variable Role in Protein Stability Uncovered by Liquid-Observed Vapor Exchange NMR.Biochemistry · 2021Article
- Electrostatic spray drying for monoclonal antibody formulation.International journal of pharmaceutics · 2021Article
- Understanding the Impact of Protein-Excipient Interactions on Physical Stability of Spray-Dried Protein Solids.Molecular pharmaceutics · 2021Article
- Pharmaceutical protein solids: Drying technology, solid-state characterization and stability.Advanced drug delivery reviews · 2021Review
- 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
- Dried Protein Structure Revealed at the Residue Level by Liquid-Observed Vapor Exchange NMR.Biochemistry · 2021Article
- Hydrogen-Deuterium Exchange Mass Spectrometry: A Novel Structural Biology Approach to Structure, Dynamics and Interactions of Proteins and Their Complexes.Life (Basel, Switzerland) · 2020Review
- Monoclonal antibody stability can be usefully monitored using the excitation-energy-dependent fluorescence edge-shift.The Biochemical journal · 2020Article
- Evaluation of Predictors of Protein Relative Stability Obtained by Solid-State Hydrogen/Deuterium Exchange Monitored by FTIR.Pharmaceutical research · 2020Article
- 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 the antibiotic component on in-vitro bacterial killing, physico-chemical properties, aerosolization and dissolution of a ternary-combinational inhalation powder formulation of antibiotics for pan-drug resistant Gram-negative lung infections.International journal of pharmaceutics · 2019Article
- Probing Conformational Diversity of Fc Domains in Aggregation-Prone Monoclonal Antibodies.Pharmaceutical research · 2018Article
- Effects of Drying Process on an IgG1 Monoclonal Antibody Using Solid-State Hydrogen Deuterium Exchange with Mass Spectrometric Analysis (ssHDX-MS).Pharmaceutical research · 2018Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Solid state amide hydrogen/deuterium exchange with mass spectrometric analysis (ssHDX-MS) was used to assess the conformation of myoglobin (Mb) in lyophilized formulations, and the results correlated with the extent of aggregation during storage. Mb was colyophilized with sucrose (1:1 or 1:8 w/w), mannitol (1:1 w/w), or NaCl (1:1 w/w) or in the absence of excipients. Immediately after lyophilization, samples of each formulation were analyzed by ssHDX-MS and Fourier transform infrared spectroscopy (FTIR) to assess Mb conformation, and by dynamic light scattering (DLS) and size exclusion chromatography (SEC) to determine the extent of aggregation. The remaining samples were then placed on stability at 25 °C and 60% RH or 40 °C and 75% RH for up to 1 year, withdrawn at intervals, and analyzed for aggregate content by SEC and DLS. In ssHDX-MS of samples immediately after lyophilization (t = 0), Mb was less deuterated in solids containing sucrose (1:1 and 1:8 w/w) than in those containing mannitol (1:1 w/w), NaCl (1:1 w/w), or Mb alone. Deuterium uptake kinetics and peptide mass envelopes also indicated greater Mb structural perturbation in mannitol, NaCl, or Mb-alone samples at t = 0. The extent of deuterium incorporation and kinetic parameters related to rapidly and slowly exchanging amide pools (Nfast, Nslow), measured at t = 0, were highly correlated with the extent of aggregation on storage as measured by SEC. In contrast, the extent of aggregation was weakly correlated with FTIR band intensity and peak position measured at t = 0. The results support the use of ssHDX-MS as a formulation screening tool in developing lyophilized protein drug products.
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