ArticleAnalytical chemistry2018
Hydrolysis-Kinetic Study of AEBSF, a Protease Inhibitor Used during Cell-Culture Processing of the HIV-1 Broadly Neutralizing Antibody CAP256-VRC25.26.
Article in Analytical chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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
5 citing papers in PubMed.
- Covalent Protein Inhibitors via Tyrosine and Tryptophan Conjugation with Cyclic Imine Mannich Electrophiles.Angewandte Chemie (International ed. in English) · 2026Article
- Human Neutrophil Elastase: Characterization of Intra- vs. Extracellular Inhibition.International journal of molecular sciences · 2024Article
- Characterization of AEBSF-antibody modifications for a protease inhibitor supplementation strategy.Analytical and bioanalytical chemistry · 2019Article
- Quantification of residual AEBSF-related impurities by reversed-phase liquid chromatography.Journal of chromatography. B, Analytical technologies in the biomedical and life sciences · 2019Article
- Sulfonamide Synthesis via Calcium Triflimide Activation of Sulfonyl Fluorides.Organic letters · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
Abstract
One approach to mitigate product clipping during HIV mAb CAP256-VRC26.25 cell-culture development is the addition of the protease inhibitor 4-(2-aminoethyl) benzenesulfonyl fluoride (AEBSF) to the cell-culture media. AEBSF can undergo hydrolysis to form an inactive compound, 4-(2-aminoethyl) benzenesulfonic acid. Using mass-spectrometry detection, a kinetic profile of AEBSF hydrolysis was generated for conditions simulating those of cell culture at pH 7.0 and 37 °C. It was found that increasing the pH or the temperature could accelerate AEBSF hydrolysis. The kinetic-study results in this report provide an analytical characterization and guidance when optimizing an AEBSF-addition strategy for product-clipping control during cell-culture development and offer an alternative approach for AEBSF-related clearance studies post protein production.
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Registered trials
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