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2000
Volume 22, Issue 9
  • ISSN: 1389-2010
  • E-ISSN: 1873-4316

Abstract

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 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-α on the membrane for 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 the addition of TNF-α to cultivation media. Conclusion: These results suggest that affibody molecules against TNF-α could be candidate molecules for the detection of TNF-α during biochemical analysis and pharmacotherapy for rheumatoid arthritis.

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/content/journals/cpb/10.2174/1389201021666201016143730
2021-07-01
2025-04-23
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  • Article Type:
    Research Article
Keyword(s): Affibody; IL-6; MMP-3; Rheumatoid Arthritis (RA); synovial cell; TNF-α
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