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A Novel Phage-Library-Selected Peptide Inhibits Human TNF-α Binding to Its Receptors
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-produc...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6271742/ https://www.ncbi.nlm.nih.gov/pubmed/24896264 http://dx.doi.org/10.3390/molecules19067255 |
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author | Brunetti, Jlenia Lelli, Barbara Scali, Silvia Falciani, Chiara Bracci, Luisa Pini, Alessandro |
author_facet | Brunetti, Jlenia Lelli, Barbara Scali, Silvia Falciani, Chiara Bracci, Luisa Pini, Alessandro |
author_sort | Brunetti, Jlenia |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-6271742 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-62717422018-12-21 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 Molecules Article 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. MDPI 2014-06-03 /pmc/articles/PMC6271742/ /pubmed/24896264 http://dx.doi.org/10.3390/molecules19067255 Text en © 2014 by the authors. licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). |
spellingShingle | Article Brunetti, Jlenia Lelli, Barbara Scali, Silvia Falciani, Chiara Bracci, Luisa Pini, Alessandro A Novel Phage-Library-Selected Peptide Inhibits Human TNF-α Binding to Its Receptors |
title | A Novel Phage-Library-Selected Peptide Inhibits Human TNF-α Binding to Its Receptors |
title_full | A Novel Phage-Library-Selected Peptide Inhibits Human TNF-α Binding to Its Receptors |
title_fullStr | A Novel Phage-Library-Selected Peptide Inhibits Human TNF-α Binding to Its Receptors |
title_full_unstemmed | A Novel Phage-Library-Selected Peptide Inhibits Human TNF-α Binding to Its Receptors |
title_short | A Novel Phage-Library-Selected Peptide Inhibits Human TNF-α Binding to Its Receptors |
title_sort | novel phage-library-selected peptide inhibits human tnf-α binding to its receptors |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6271742/ https://www.ncbi.nlm.nih.gov/pubmed/24896264 http://dx.doi.org/10.3390/molecules19067255 |
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