ArticleResearch in pharmaceutical sciences
Optimization of a single-chain antibody fragment overexpression in Escherichia coli using response surface methodology.
Article in Research in pharmaceutical sciences. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 35 citations in OpenAlex.
- An Optimized and Systematically Integrated Expression, Extraction, and Purification Strategy Enabling Efficient Production of TCR-Like Antibodies in Escherichia coli.Current microbiology · 2026Article
- Enhancing soluble expression and purification of a bispecific scFv antibody inResearch in pharmaceutical sciences · 2026Article
- Integrated bioprocessing and genetic strategies to enhance soluble expression of anti-HER2 immunotoxin in E. Coli.AMB Express · 2024Article
- Enhanced production of a recombinant xylanase (XT6): optimization of production and purification, and scaled-up batch fermentation in a stirred tank bioreactor.Scientific reports · 2023Article
- Implementation of a Design of Experiments to Improve Periplasmic Yield of Functional ScFv Antibodies in a Phage Display Platform.Advanced pharmaceutical bulletin · 2022Article
- Statistical optimization of culture conditions for expression of recombinant humanized anti-EpCAM single-chain antibody using response surface methodology.Research in pharmaceutical sciences · 2021Article
- RSM-based Model to Predict Optimum Fermentation Conditions for Soluble Expression of the Antibody Fragment Derived from 4D5MOC-B Humanized Mab in SHuffle™ T7Iranian journal of pharmaceutical research : IJPR · 2021Article
- Optimization of solvent media to solubilize TEV protease using response surface method.Research in pharmaceutical sciences · 2020Article
- Evaluation of soluble expression of recombinant granulocyte macrophage stimulating factor (rGM-CSF) by three differentResearch in pharmaceutical sciences · 2020Article
- Optimization of Buffer Additives for Efficient Recovery of hGM-CSF from Inclusion Bodies Using Response Surface Methodology.Iranian journal of pharmaceutical research : IJPR · 2020Article
- Anti-HER2 scFv Expression in Escherichia coli SHuffleMolecular biotechnology · 2020Article
- Perspectives of inclusion bodies for bio-based products: curse or blessing?Applied microbiology and biotechnology · 2019Review
- High-yield Production of Granulocyte-macrophage Colony-stimulating Factor inIranian journal of pharmaceutical research : IJPR · 2019Article
- Improvement of solubility and refolding of an anti-human epidermal growth factor receptor 2 single-chain antibody fragment inclusion bodies.Research in pharmaceutical sciences · 2018Article
- Optimization of physical conditions for the production of thermostable T1 lipase in Pichia guilliermondii strain SO using response surface methodology.BMC biotechnology · 2017Article
- Optimization of the Expression of DT386-BR2 Fusion Protein inAdvanced biomedical research · 2017Article
- Expression and Secretion of Endostar Protein by Escherichia Coli: Optimization of Culture Conditions Using the Response Surface Methodology.Molecular biotechnology · 2016Article
- Effect of Culture Condition Variables on Human Endostatin Gene Expression inJundishapur journal of microbiology · 2016Article
- Hybrid modeling as a QbD/PAT tool in process development: an industrial E. coli case study.Bioprocess and biosystems engineering · 2016Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human epidermal growth factor receptor (HER) family plays an important role in various types of cancers. As a result, antibodies against HER and the mechanism of antigen-antibody binding action are under active investigation. We previously constructed a single-chain variable fragment (ScFv) against HER2, i.e. anti-Her2 ScFv, for expressing in the Escherichia coli. In the present study, we report the optimization of anti-Her2 ScFv expression in an E. coli host of BL21 (DE3) pLysS using response surface methodology based on tuning of three cultivation variables, including isopropyl-beta-D-thiogalactopyranoside (IPTG) concentration, temperature and post-induction time. A model for protein expression according to the Box-Behnken design predicted a maximal anti-Her2 ScFv expression at 37 °C, a post-induction time of 10.45 h and 0.75 mM IPTG. In addition, strategies based on inclusion body isolation and affinity chromatography were applied to purify anti-Her2 ScFv. The purity of the final product for inclusion bodies isolation and purification by Ni-NTA resin were 70 % and 95 %, respectively. The solubilization of the inclusion bodies was carried out using two denaturant agents, guanidine hydrochloride and urea. The present study showed that guanidine hydrochloride was more effective than urea in solubilizing the inclusion bodies.
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26430460PMC4578215W2339542797What 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.