ArticlemAbs
Aggregation of biopharmaceuticals in human plasma and human serum: implications for drug research and development.
Article in mAbs. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 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.
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Who cites it
15 citing papers in PubMed, 41 citations in OpenAlex.
- Unraveling the Effects of Filtration, Process Interruptions, and Post-Process Agitation on Protein Aggregation.AAPS PharmSciTech · 2025Article
- Novel semi-automated fluorescence microscope imaging algorithm for monitoring IgG aggregates in serum.Scientific reports · 2021Article
- Micro-Heterogeneity of Antibody Molecules.Experientia supplementum (2012) · 2021Review
- In Vivo Stability of Therapeutic Proteins.Pharmaceutical research · 2020Review
- Considerations for the Design of Antibody-Based Therapeutics.Journal of pharmaceutical sciences · 2020Review
- Submicron Protein Particle Characterization using Resistive Pulse Sensing and Conventional Light Scattering Based Approaches.Pharmaceutical research · 2018Article
- Article
- Cancer Chemotherapy Update: Bevacizumab, Etoposide, and Cisplatin Regimen for Refractory Brain Metastases.Hospital pharmacy · 2017Article
- Article
- Posttranslational Modifications and the Immunogenicity of Biotherapeutics.Journal of immunology research · 2016Review
- Article
- Selective assembly of DNA-conjugated single-walled carbon nanotubes from the vascular secretome.ACS nano · 2014Article
- Quality control and stability studies with the monoclonal antibody, trastuzumab: application of 1D- vs. 2D-gel electrophoresis.International journal of molecular sciences · 2014Article
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- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Analytical methods based on light microscopy, 90° light-scattering and surface plasmon resonance (SPR) allowed the characterization of aggregation that can occur when antibodies are mixed with human plasma. Light microscopy showed that aggregates formed when human plasma was mixed with 5% dextrose solutions of Herceptin(®) (trastuzumab) or Avastin(®) (bevacizumab) but not Remicade(®) (infliximab). The aggregates in the plasma-Herceptin(®)-5% dextrose solution were globular, size range 0.5-9 μm, with a mean diameter of 4 μm. The aggregates in the plasma-Avastin(®)-5% dextrose samples had a mean size of 2 μm. No aggregation was observed when 0.9% NaCl solutions of Herceptin(®), Avastin(®) and Remicade(®) were mixed with human plasma. 90° light-scattering measurements showed that aggregates were still present 2.5 h after mixing Herceptin(®) or Avastin(®) with 5% dextrose-plasma solution. A SPR method was utilized to qualitatively describe the extent of interactions of surface-bound antibodies with undiluted human serum. Increased binding was observed in the case of Erbitux(®) (cetuximab), whereas no binding was measured for Humira(®) (adalimumab). The binding of sera components to 13 monoclonal antibodies was measured and correlated with known serum binding properties of the antibodies. The data presented in this paper provide analytical methods to study the intrinsic and buffer-dependent aggregation tendencies of therapeutic proteins when mixed with human plasma and serum.
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What OpenQuestion holds
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.