Synthetic C-terminal peptide of IL-1 functions as a binding domain as well as an antagonist for the IL-1 receptor.
Fragments of IL-1 beta were chemically synthesized and tested for biological activity as well as binding of radiolabelled peptides to the IL-1 receptor. A peptide from the extreme C-terminal region of IL-1 beta was found to antagonize intact, native IL-1 beta in the thymocyte bioassay. In addition, this C-terminal region peptide, when radiolabelled, can function as a ligand for the IL-1 receptor on murine cell lines and effectively compete with intact radiolabelled recombinant IL-1 beta.
D000818:Animals; D001665:Binding Sites; D001667:Binding, Competitive; D001681:Biological Assay; D002460:Cell Line; D006801:Humans; D007375:Interleukin-1 / Q000037:antagonists & inhibitors / Q000378:metabolism*; D051379:Mice; D010446:Peptide Fragments / Q000378:metabolism; D011869:Radioligand Assay; D011971:Receptors, Immunologic / Q000378:metabolism*; D017472:Receptors, Interleukin-1; D011994:Recombinant Proteins / Q000378:metabolism; D013329:Structure-Activity Relationship
D007375:Interleukin-1; D010446:Peptide Fragments; D011971:Receptors, Immunologic; D017472:Receptors, Interleukin-1; D011994:Recombinant Proteins