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.
|Titolo:||A novel phage-library-selected peptide inhibits human TNF-α binding to its receptors|
|Citazione:||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.|
|Appare nelle tipologie:||1.1 Articolo in rivista|