ArticleBiophysical journal2008
Protein conformation in amorphous solids by FTIR and by hydrogen/deuterium exchange with mass spectrometry.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 36 citations in OpenAlex.
- Structural Instability of Human Serum Albumin during Microparticles Synthesis.ACS applied bio materials · 2025Article
- Understanding dry proteins and their protection with solid-state hydrogen-deuterium exchange.Protein science : a publication of the Protein Society · 2025Review
- Analytical Techniques for Structural Characterization of Proteins in Solid Pharmaceutical Forms: An Overview.Pharmaceutics · 2021Review
- Evaluation of Predictors of Protein Relative Stability Obtained by Solid-State Hydrogen/Deuterium Exchange Monitored by FTIR.Pharmaceutical research · 2020Article
- 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
- On-tissue Direct Monitoring of Global Hydrogen/Deuterium Exchange by MALDI Mass Spectrometry: Tissue Deuterium Exchange Mass Spectrometry (TDXMS).Molecular & cellular proteomics : MCP · 2016Article
- Mass spectrometric approaches to study protein structure and interactions in lyophilized powders.Journal of visualized experiments : JoVE · 2015Article
- 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. 2. Exchange kinetics.Molecular pharmaceutics · 2012Article
- Localized hydration in lyophilized myoglobin by hydrogen-deuterium exchange mass spectrometry. 1. Exchange mapping.Molecular pharmaceutics · 2012Article
- Use of glass transitions in carbohydrate excipient design for lyophilized protein formulations.Computers & chemical engineering · 2012Article
- Facile formation of dynamic hydrogel microspheres for triggered growth factor delivery.Acta biomaterialia · 2011Article
- Correlation to protein conformation of Wide-angle X-ray Scatter parameters.The protein journal · 2010Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Solid-state hydrogen/deuterium exchange (ssHDX) with electrospray ionization mass spectrometry (ESI-MS) and Fourier transform infrared (FTIR) spectroscopy were used to assess protein conformation in amorphous solids. Myoglobin, lysozyme, beta-lactoglobulin, ribonuclease A, E-cadherin 5, and concanavalin A were co-lyophilized with carbohydrates (trehalose, raffinose, and dextran 5000), linear polymers (polyvinyl alcohol and polyvinyl pyrrolidone) or guanidine hydrochloride (negative control). For ssHDX, samples were exposed to D2O vapor at 33% relative humidity and room temperature, and then reconstituted at low temperature (4 degrees C) and pH 2.5 and analyzed by ESI-MS. Peptic digestion of selected proteins was used to provide region-specific information on exchange. FTIR spectra were acquired using attenuated total reflectance. FTIR and ssHDX of intact proteins showed preservation of structure by raffinose and trehalose, as indicated by FTIR band intensity and protection from exchange. ssHDX of peptic digests further indicated that these protective effects were not exerted uniformly along the protein sequence but were observed primarily in alpha-helical regions, a level of structural resolution not afforded by FTIR. The results thus demonstrate the utility of HDX with ESI-MS for analyzing protein conformation in amorphous solid samples.
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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.