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• W2093233631 abstract "Phage displayed peptide library was used to select tumor necrosis factor α (TNFα) binding peptides. After three sequential rounds of biopanning, some linear TNFα-binding peptides were identified from a 12-mer peptide library. A consensus sequence (L/M)HEL(Y/F)(L/M)X(W/Y/F), where X might be variable residue, was deduced from sequences of these peptides. The phages bearing these peptides showed specific binding to immobilized TNFα, with over 80% of phages bound being competitively eluted by free TNFα. To confirm the binding activity and to explore further functional properties, three peptides with typical structure were selected and expressed as GST-fused protein. These recombinant peptides effectively competed for [125I]TNFα binding to TNFR1 in a dose-dependent manner, with IC50 from 10 to 160 μM. Furthermore, the GST-fused derivatives showed inhibitory effects on TNFα-induced cytotoxicity. Taken together, these data demonstrate that the TNFα-binding peptides are effective antagonists of TNFα and the deduced motif might be useful in development of novel low molecular weight anti-TNFα drugs." @default.
• W2093233631 created "2016-06-24" @default.
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• W2093233631 date "2003-10-01" @default.
• W2093233631 modified "2023-09-27" @default.
• W2093233631 title "Identification of anti-TNFα peptides with consensus sequence" @default.
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• W2093233631 doi "https://doi.org/10.1016/j.bbrc.2003.09.141" @default.
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