ArticleAdvanced pharmaceutical bulletin2015
Identification of Novel Single Chain Fragment Variable Antibodies Against TNF-α Using Phage Display Technology.
Article in Advanced pharmaceutical bulletin, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 9 citations in OpenAlex.
- Characterization of Novel Fragment Antibodies Against TNF-alpha Isolated Using Phage Display Technique.Iranian journal of pharmaceutical research : IJPR · 2019Article
- A Novel Single Domain Antibody Targeting FliC Flagellin ofFrontiers in microbiology · 2019Article
- Isolation and Characterization of Novel Phage Displayed scFv Fragment for Human Tumor Necrosis Factor Alpha and Molecular Docking Analysis of Their Interactions.Iranian journal of pharmaceutical research : IJPR · 2018Article
- A Novel Fully Human Agonistic Single Chain Fragment Variable Antibody Targeting Death Receptor 5 with Potent Antitumor Activity In Vitro and In Vivo.International journal of molecular sciences · 2017Article
- Prokaryotic expression of MLAA-34 and generation of a novel human ScFv against MLAA-34 by phage display technology.Oncotarget · 2017Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
purposeTumor necrosis factor alpha (TNF-α) is an inflammatory cytokine, involved in both physiological and pathological pathways. Because of central role of TNF-α in pathogenesis of inflammatory diseases, in the current study, we aimed to identify novel scFv antibodies against TNF-α using phage display technology.
methodsUsing libraries composed of phagemid displaying scFv antibodies, four rounds of biopanning against TNF-α were carried out, which led to identification of scFvs capable of binding to TNF-α. The scFv antibody with appropriate binding affinity towards TNF-α, was amplified and used in ELISA experiment.
resultsTitration of phage achieved from different rounds of biopanning showed an enrichment of specific anti-TNF-α phages during biopanning process. Using ELISA experiment, a binding constant (Kd) of 1.11 ± 0.32 nM was determined for the phage displaying J48 scFv antibody.
conclusionThe findings in the current work revealed that the identified novel scFv antibody displayed at the N-terminal of minor coat proteins of phagemid binds TNF-α with suitable affinity. However, the soluble form of the antibody is needed to be produced and evaluated in more details regarding its binding properties to TNF-α.
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Registered trials
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