ArticleJournal of pharmaceutical sciences2015
Transmission electron microscopy as an orthogonal method to characterize protein aggregates.
Article in Journal of pharmaceutical sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
22 citing papers in PubMed, 61 citations in OpenAlex.
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- Structural Characteristics and Properties of the RNA-Binding Protein hnRNPK at Multiple Physical States.International journal of molecular sciences · 2025Article
- Three dimensional visualization of subcellular and suborganellar structures in near-native plant cells by synchrotron soft X-ray tomography.Frontiers in plant science · 2025Article
- Exosomes isolation from bovine serum: qualitative and quantitative comparison between ultracentrifugation, combination ultracentrifugation and size exclusion chromatography, and exoEasy methods.Journal of animal science and technology · 2024Article
- Soybean isolate protein complexes with different concentrations of inulin by ultrasound treatment: Structural and functional properties.Ultrasonics sonochemistry · 2024Article
- Formation of Calprotectin Inhibits Amyloid Aggregation of S100A8 and S100A9 Proteins.ACS chemical neuroscience · 2024Article
- Synergistic Assembly of 1DZnO and Anti-CYFRA 21-1: A Physicochemical Approach to Optical Biosensing.BME frontiers · 2024Article
- Multiple sclerosis plasma IgG aggregates induce complement-dependent neuronal apoptosis.Cell death & disease · 2023Article
- Protein quality control and aggregation in the endoplasmic reticulum: From basic to bedside.Frontiers in cell and developmental biology · 2023Review
- An Interlaboratory Comparison on the Characterization of a Sub-micrometer Polydisperse Particle Dispersion.Journal of pharmaceutical sciences · 2022Article
- Antioxidative Activity of Soy, Wheat and Pea Protein Isolates Characterized by Multi-Enzyme Hydrolysis.Nanomaterials (Basel, Switzerland) · 2021Article
- Particle Detection and Characterization for Biopharmaceutical Applications: Current Principles of Established and Alternative Techniques.Pharmaceutics · 2020Review
- The Stability Maintenance of Protein Drugs in Organic Coatings Based on Nanogels.Pharmaceutics · 2020Article
- Electron microscopy-based semi-automated characterization of aggregation in monoclonal antibody products.Computational and structural biotechnology journal · 2020Article
- Measurement of Average Aggregate Density by Sedimentation and Brownian Motion Analysis.Journal of pharmaceutical sciences · 2018Article
- Characterization of ELISA Antibody-Antigen Interaction using Footprinting-Mass Spectrometry and Negative Staining Transmission Electron Microscopy.Journal of the American Society for Mass Spectrometry · 2018Article
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
Abstract
Aggregation of protein-based therapeutics is a challenging problem in the biopharmaceutical industry. Of particular concern are implications for product efficacy and clinical safety because of potentially increased immunogenicity of the aggregates. We used transmission electron microscopy (TEM) to characterize biophysical and morphological features of antibody aggregates formed upon controlled environmental stresses. TEM results were contrasted with results obtained in parallel by independent methods, including size-exclusion chromatography, dynamic light scattering, microflow imaging, and nanoparticle tracking. For TEM, stressed samples were imaged by negative staining and in the frozen-hydrated state. In both cases, aggregates appeared amorphous but differed in fine structural detail. Specifically, negatively stained aggregates were compact and consisted of smaller globular structures that had a notable three-dimensional character. Elements of the native IgG structure were retained, suggesting that the aggregates were not assembled from denatured protein. In contrast, aggregates in frozen-hydrated samples appeared as extended, branched protein networks with large surface area. Using multiple scales of magnification, a wide range of particle sizes was observed and semiquantitatively characterized. The detailed information provided by TEM extended observations obtained with the independent methods, demonstrating the suitability of TEM as a complementary approach to submicron particle analysis.
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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.