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Functional Evaluation of anti-TNF-α Antibody Molecules in Biochemical Detection and Inhibition to Signalling Pathways of a Synovial Cell.
Current Pharmaceutical Biotechnology 2020 October 17
BACKGROUND: An affibody molecule obtained from a bioengineered staphylococcal protein was previously shown to act as an affinity binder for a wide range of targets and to develop tumour necrosis factor α (TNF-α-binding clones).
METHODS: In this study, we demonstrated that affibody molecules against TNF-α could bind to recombinant TNF- on the membrane for a biochemical detection. In addition, we examined whether the affibody molecules could block binding between recombinant TNF-α and its receptor on MH7A synovial cells.
RESULTS: When a TNF-α-binding affibody was added, the production level of inflammatory mediators IL-6 and MMP-3 in MH7A were found to decrease up to 44%. Additionally, proliferation of synovial cells was also inhibited by addition of TNF-α to the cultivation media.
CONCLUSION: These results suggest that affibody molecules against TNF-α could be candidate molecules for the detection of TNF- during biochemical analysis and pharmacotherapy for rheumatoid arthritis.
METHODS: In this study, we demonstrated that affibody molecules against TNF-α could bind to recombinant TNF- on the membrane for a biochemical detection. In addition, we examined whether the affibody molecules could block binding between recombinant TNF-α and its receptor on MH7A synovial cells.
RESULTS: When a TNF-α-binding affibody was added, the production level of inflammatory mediators IL-6 and MMP-3 in MH7A were found to decrease up to 44%. Additionally, proliferation of synovial cells was also inhibited by addition of TNF-α to the cultivation media.
CONCLUSION: These results suggest that affibody molecules against TNF-α could be candidate molecules for the detection of TNF- during biochemical analysis and pharmacotherapy for rheumatoid arthritis.
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