Screening of an oligopeptide antagonist for interleukin-6 from a random phage library View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2000-06

AUTHORS

Hiroshi Mizuguchi, Tomoko Kubomi, Rina Nomura, Kiyoshi Yasukawa, Tadayuki Imanaka, Masahiro Takagi

ABSTRACT

To develop a small peptide antagonist for a cytokine, an oligopeptide ligand interacting with interleukin-6 (IL-6) has been screened by affinity panning from a random heptapeptide displaying phage library. After biopanning five times against IL-6, ten phages displaying heptapeptides with consensus sequence, K(L/V)WXIPQ, were selected out of nucleotide sequencing of 21 phages. A synthetic oligopeptide, KLWTIPQ (P-1), was prepared but it did not inhibit growth of MH60, an IL-6 dependent cell line. To stabilize the structure of oligopeptide and bring stronger molecular hindrance In interaction between IL-6 and its two receptors (IL-6R and gp130), a peptide with two cysteine residues at each end of consensus sequence, GGCKLWTIPQCGG (PC), was also synthesized, which significantly inhibited cell growth of MH60 at over 100 μM and phosphorylation of Stat3, which is primary signal transducer and activator of transcription, phosphorylated by IL-6 signal. These results strongly suggest that PC is specifically bound to IL-6 and hinders formation of IL-6/IL-6R/gp130 complex. More... »

PAGES

1015-1020

Identifiers

URI

http://scigraph.springernature.com/pub.10.1023/a:1005605808186

DOI

http://dx.doi.org/10.1023/a:1005605808186

DIMENSIONS

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