Antagonistic effect of disulfide-rich peptide aptamers selected by cDNA display on interleukin-6-dependent cell proliferation

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• 作者：Naoto Nemoto^a ; ^b ; ^c ; ^{nemoto@fms.saitama-u.ac.jp} ; Chihiro Tsutsui^a ; ¹ ; Junichi Yamaguchi^b ; ^d ; ² ; Shingo Ueno^a ; Masayuki Machida^d ; Toshikatsu Kobayashi^b ; ^c ; Takafumi Sakai^a
• 关键词：Peptide aptamer ; Protein scaffold ; Cysteine knot miniprotein ; mRNA/cDNA display ; In vitro selection ; IL-6
• 刊名：Biochemical and Biophysical Research Communications
• 出版年：2012
• 出版时间：27 April, 2012
• 年：2012
• 卷：421
• 期：1
• 页码：129-133
• 全文大小：548 K

文摘

Several engineered protein scaffolds have been developed recently to circumvent particular disadvantages of antibodies such as their large size and complex composition, low stability, and high production costs. We previously identified peptide aptamers containing one or two disulfide-bonds as an alternative ligand to the interleukin-6 receptor (IL-6R). Peptide aptamers (32 amino acids in length) were screened from a random peptide library by in vitro peptide selection using the evolutionary molecular engineering method ¡°cDNA display? In this report, the antagonistic activity of the peptide aptamers were examined by an in vitro competition enzyme-linked immunosorbent assay (ELISA) and an IL-6-dependent cell proliferation assay. The results revealed that a disulfide-rich peptide aptamer inhibited IL-6-dependent cell proliferation with similar efficacy to an anti-IL-6R monoclonal antibody.