Whole cell-based surface plasmon resonance measurement to assess binding of anti-TNF agents to transmembrane target
| Autor: | Takeharu Ogura, Yoshiyuki Tanaka, Hiromu Toyoda |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Analyte Necrosis Stereochemistry Biophysics Biochemistry Jurkat cells Chemistry Techniques Analytical Etanercept Cell membrane 03 medical and health sciences Jurkat Cells 0302 clinical medicine medicine Humans Surface plasmon resonance Receptor Molecular Biology Chemistry Tumor Necrosis Factor-alpha Cell Membrane Adalimumab Antibodies Monoclonal Cell Biology Surface Plasmon Resonance Transmembrane protein Infliximab 030104 developmental biology medicine.anatomical_structure 030220 oncology & carcinogenesis Antirheumatic Agents Tumor necrosis factor alpha medicine.symptom Carrier Proteins Protein Binding |
| Zdroj: | Analytical biochemistry. 508 |
| ISSN: | 1096-0309 |
| Popis: | We developed a technique for the measurement of surface plasmon resonance (SPR) to detect interactions of anti-tumor necrosis factor (TNF) agents with transmembrane TNF-α (mTNF-α) on living whole cells. The injection of a suspension of mTNF-α expressing Jurkat cells, used as an analyte, gave a clear binding response to anti-TNF agents, such as etanercept, infliximab and adalimumab, immobilized on sensorchip. The binding response of the analyte cells increased in a concentration-dependent manner and was competitively reduced by adding soluble TNF receptors to the analyte cell suspension. Treatment of analyte cells with free anti-TNF agent before injection reduced the binding response between the analyte cells and immobilized-etanercept on sensorchip, and the inhibitory effect of free anti-TNF agent was concordant with the affinity of anti-TNF agent for soluble TNF-α. These findings indicate that the SPR response arises from specific binding between anti-TNF agent and its target on cell membrane. |
| Databáze: | OpenAIRE |
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