Functional Evaluation of Anti-TNF-α Affibody Molecules in Biochemical Detection and Inhibition to Signalling Pathways of a Synovial Cell

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 alpha (TNF-alpha)-binding clones. Methods: In this study, we demonstrated that affibody molecules against TNF-alpha could bind to recombinant TNF-alpha on the membrane for biochemical detection. In addition, we examined whether the affibody molecules could block binding between recombinant TNF-alpha and its receptor on MH7A synovial cells. Results: When a TNF-alpha-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-alpha to cultivation media. Conclusion: These results suggest that affibody molecules against TNF-alpha could be candidate molecules for the detection of TNF-alpha during biochemical analysis and pharmacotherapy for rheumatoid arthritis.

Automated summary

The affibody molecules targeting TNF-alpha demonstrated binding to recombinant TNF-alpha for biochemical detection and blocking of TNF-alpha from binding to its receptor on MH7A synovial cells. These affibody molecules showed potential in decreasing inflammatory mediators production and inhibiting synovial cells proliferation, suggesting their application in biochemical analysis and pharmacotherapy for rheumatoid arthritis.