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A synthetic complement C1q-like peptide selectively interacts with immune complexes

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Abstract

A water-soluble peptide possessing an immune complex selective affinity was synthesized and its primary structure established as: Leu-Glu-Gln-Gly-Glu-Asn-Val-Phe-Leu-Gln-Ala-Thr-Ser-Asp-Asp-Cys. This peptide, designated as C1q-like peptide (CLP), represents a possible immune complex binding epitope of complement C1q. CLP has a hydrophilicity value of 0.21. At 0.5 μM, it inhibited by 50% natural human C1q from binding to horseradish peroxidase-rabbit anti-peroxidase immune complex. CLP failed to inhibit Staphylococcus aureus protein A from binding monomeric IgG. When coated to a microplate, CLP showed selective binding to the immune complex, and could be used for application in immunochemical detection of immune complex. © Rapid Science Ltd. 1998

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Authors and Affiliations

  1. Institute of Biological Science and Technology, National Chiao Tung University, Taoyuan, Taiwan

    C. Allen Chang

  2. Institute of Biotechnology, National Dong-Hwa University, Taoyuan, Taiwan

    Tzong-Zeng Wu & Yong-Bing Kuo

  3. School of Medical Technology, Chang Gung University, Taoyuan, Taiwan

    Err-Cheng Chan & Mai-Zon Pan

Authors
  1. Err-Cheng Chan
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  2. Mai-Zon Pan
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  3. C. Allen Chang
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  4. Tzong-Zeng Wu
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  5. Yong-Bing Kuo
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Chan, EC., Pan, MZ., Chang, C.A. et al. A synthetic complement C1q-like peptide selectively interacts with immune complexes. Biotechnology Letters 20, 1119–1123 (1998). https://doi.org/10.1023/A:1005368118207

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  • DOI: https://doi.org/10.1023/A:1005368118207

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