Studies on Peptides. CLXVII. / Solid-Phase Syntheses and Immunological Properties of Fragment Peptides Related to Human Malaria Circumsporozoite Protein

  • 赤路 健一
    Faculty of Pharmaceutical Sciences, Kyoto University
  • 林 良雄
    Faculty of Pharmaceutical Sciences, Kyoto University
  • 藤井 信孝
    Faculty of Pharmaceutical Sciences, Kyoto University
  • 劉 徳勇
    Office of Biologics Research and Review, Food and Drug Administration
  • BERKOWER Ira
    Office of Biologics Research and Review, Food and Drug Administration
  • 矢島 治明
    Faculty of Pharmaceutical Sciences, Kyoto University

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A glycine-linked tetramer of Asn-Ala-Asn-Pro, a tandem repeated sequence of malaria circumsporozoite (CS) protein, was synthesized by the Boc-based solid phase method, followed by deprotection with 1 M trimethylsilyl trifluotomethanesulfonate-thioanisole in trifluoroacetic acid. In addition, three tetramer-related peptides were similarly synthesized, i. e., a 34-residue peptide [linked with TH, a proposed T-cell epitope of CS, at the C-terminus of the tetramer], a 46-residue peptide and a 59-residue peptide [linked with HA or HA', two preposed T-cell epitopes of influenza hemagglutinin protein, at the N-terminus of the above 34-residue peptide]. Their immunological properties were examined by enzyme-linked immunosorbent assay, for which three different congenic strains of mouse were used to raise the specific antibodies. Despite conjugation of T-cell epitopes to the tetramer, the mice of low-responder strains to the tetramer failed to produce any antibody specific to the tetramer. However, with the aid of recombinant interleukin 2 as an adjuvant, the low-responder mice produced antibody with relatively high titers.

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