A Novel Phage-Library-Selected Peptide Inhibits Human TNF-α Binding to Its Receptors

Molecules

Jlenia Brunetti¹  Barbara Lelli¹  Silvia Scali¹  Chiara Falciani²  Luisa Bracci¹ 

[1]Department of Medical Biotechnologies, University of Siena, Via A. Moro 2, 53100 Siena, Italy

[2] E-Mails:

[3]SetLance srl, via Fiorentina 1, 53100 Siena, Italy

[4] E-Mail:

关键词: TNF-α;    anti-TNF-α peptide;    branched peptides;    phage display;    solid-phase synthesis;    competitive selection;    surface plasmon resonance;   

DOI  :  10.3390/molecules19067255

来源: mdpi

【 摘 要 】

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.

【 授权许可】

CC BY   
© 2014 by the authors; licensee MDPI, Basel, Switzerland.