ArticleTechnology in cancer research & treatment2017
Sensitive Detection of Immunoglobulin G Stability Using in Real-Time Isothermal Differential Scanning Fluorimetry: Determinants of Protein Stability for Antibody-Based Therapeutics.
Article in Technology in cancer research & treatment, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 12 citations in OpenAlex.
- Applications of Differential Scanning Fluorimetry and Related Technologies in Characterization of Protein-Ligand Interactions.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Article
- In vivo deglycosylation of recombinant glycoproteins in tobacco BY-2 cells.Plant biotechnology journal · 2023Article
- Protein aggregation and immunogenicity of biotherapeutics.International journal of pharmaceutics · 2020Review
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4 authors at 1 institution in 1 country.
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Abstract
Protein instability is a major obstacle in the production and delivery of monoclonal antibody-based therapies for cancer. This study presents real-time isothermal differential scanning fluorimetry as an emerging method to evaluate the stability of human immunoglobulin G protein with high sensitivity. The stability of polyclonal human immunoglobulin G against urea-induced denaturation was assessed following: (1) oxidation by the free-radical generator 2,2-Azobis[2-amidinopropane]dihydrochloride and (2) in selected storage buffers. Significant differences in immunoglobulin G stability were detected by real-time isothermal differential scanning fluorimetry when the immunoglobulin G was stored in 1,4-Piperazinediethanesulfonic acid buffer compared to phosphate-buffered saline, with half-maximal rate of denaturation occurring at a higher urea concentration in 1,4-Piperazinediethanesulfonic acid than phosphate-buffered saline (
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