We report the identification of a new human tumor necrosis factor-alpha (TNF-α) specific peptide selected by competitive panning of a phage library. Competitive elution of phages was obtained using the monoclonal antibody adalimumab, which neutralizes pro-inflammatory processes caused by over-production of TNF-α in vivo, and is used to treat severe symptoms of rheumatoid arthritis. The selected peptide was synthesized in monomeric and branched form and analyzed for binding to TNF-α and competition with adalimumab and TNF-α receptors. Results of competition with TNF-α receptors in surface plasmon resonance and melanoma cells expressing both TNF receptors make the peptide a candidate compound for the development of a novel anti-TNF-α drug.
Brunetti, J., Lelli, B., Scali, S., Falciani, C., Bracci, L., Pini, A. (2014). A novel phage-library-selected peptide inhibits human TNF-α binding to its receptors. MOLECULES, 19(6), 7255-7268 [10.3390/molecules19067255].
A novel phage-library-selected peptide inhibits human TNF-α binding to its receptors
Brunetti, Jlenia;Lelli, Barbara;Scali, Silvia;Falciani, Chiara;Bracci, Luisa;Pini, Alessandro
2014-01-01
Abstract
We report the identification of a new human tumor necrosis factor-alpha (TNF-α) specific peptide selected by competitive panning of a phage library. Competitive elution of phages was obtained using the monoclonal antibody adalimumab, which neutralizes pro-inflammatory processes caused by over-production of TNF-α in vivo, and is used to treat severe symptoms of rheumatoid arthritis. The selected peptide was synthesized in monomeric and branched form and analyzed for binding to TNF-α and competition with adalimumab and TNF-α receptors. Results of competition with TNF-α receptors in surface plasmon resonance and melanoma cells expressing both TNF receptors make the peptide a candidate compound for the development of a novel anti-TNF-α drug.File | Dimensione | Formato | |
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https://hdl.handle.net/11365/1058455