Abstract:
:Tumour necrosis factor (TNF) is a pleiotropic cytokine which plays a central role in infection, inflammation and autoimmune diseases. Its functions are mediated through binding to high affinity cell surface receptors. An approach to modulate excessive levels of TNF-alpha in the serum is the use of soluble receptors. In this study the potential of a solid-phase combinatorial peptide library was investigated to identify peptide mimics of the binding site of the TNF-alpha receptor. One of the identified mimotopes was shown to inhibit TNF-alpha-mediated cytotoxicity in mouse L929 and in a human KYM-1D4 cell lines in a dose-dependent fashion. Characterization of the mimotope sequence by high-performance liquid chromatography and mass spectroscopy has shown that the inhibitory effect of the mimotope was dependent upon the presence of a protective MTR group on the side chains of the arginine residues in the mimotope sequence. Furthermore, antibodies to the mimotope were shown to recognize the recombinant human TNF 55-kDa receptor in an ELISA assay. These findings highlight the potential of combinatorial peptide libraries in identifying peptide mimics of the binding site of TNF-alpha receptor, which can be used as competitive inhibitors of ligand-receptor interactions.
journal_name
Cytokinejournal_title
Cytokineauthors
Chirinos-Rojas CL,Steward MW,Partidos CDdoi
10.1006/cyto.1996.0158subject
Has Abstractpub_date
1997-04-01 00:00:00pages
226-32issue
4eissn
1043-4666issn
1096-0023pii
S1043-4666(96)90158-1journal_volume
9pub_type
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