Journal of Cellular Biochemistry

Amphiphilic peptides with arginine and valine residues as siRNA carriers

Authors

  • Dong-Wook Ryu,

    1. Department of Bioengineering, College of Engineering, Hanyang University, Seoul 133-791, Korea
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  • Hyun Ah Kim,

    1. Department of Bioengineering, College of Engineering, Hanyang University, Seoul 133-791, Korea
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  • Jae Hwan Ryu,

    1. Department of Bioengineering, College of Engineering, Hanyang University, Seoul 133-791, Korea
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  • Dong Yun Lee,

    1. Department of Bioengineering, College of Engineering, Hanyang University, Seoul 133-791, Korea
    2. Institute for Bioengineering and Biopharmaceutical Research, Hanyang University, Seoul 133-791, Korea
    3. Institute of Aging Society, Hanyang University, Seoul 133-791, Korea
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  • Minhyung Lee

    Corresponding author
    1. Department of Bioengineering, College of Engineering, Hanyang University, Seoul 133-791, Korea
    2. Institute for Bioengineering and Biopharmaceutical Research, Hanyang University, Seoul 133-791, Korea
    3. Institute of Aging Society, Hanyang University, Seoul 133-791, Korea
    • Department of Bioengineering, College of Engineering, Hanyang University, 17 Haengdang-dong, Seongdong-gu, Seoul 133-791, South Korea.
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Abstract

An efficient and safe delivery carrier is required for the therapeutic application of siRNA. In this research, amphiphilic peptides with arginine and valine residues were evaluated as siRNA carriers. The peptides were composed of 1–4 arginine-blocks and 6 valine-blocks. In the aqueous solution, the arginine–valine peptides (RV peptides) formed micelles with hydrophobic cores comprised of a valine block and a cationic surface comprised of an arginine block. In a gel retardation assay, the RV peptides completely retarded siRNA at a 1:10 weight ratio (siRNA:peptide). A heparin competition assay suggested that the RV peptides formed more stable complexes with siRNA than they did with polyethylenimine (25 kDa, PEI25k). In an in vitro silencing assay, a dual luciferase expression (Renilla and firefly luciferases) vector, psiCHECK2, was co-transfected into human embryonic kidney 293 cells with Renilla-siRNA using the RV peptides. The specific silencing effect of Renilla luciferase was analyzed in reference to firefly luciferase. The results showed that the R3V6 peptide was more efficient than the R1V6, R2V6, and R4V6 peptides in silencing Renilla luciferase. In the flow cytometry and in vitro silencing studies, the R3V6 peptide delivered Renila-siRNA as efficiently as PEI25k. The siVEGF/R3V6 peptide also reduced endogenous vascular endothelial growth factor (VEGF) expression in CT27 cells as efficiently as PEI25k. A cytotoxicity assay showed that RV peptides did not cause any cytotoxicity. Therefore, RV peptides may be useful for the development of a safe and efficient delivery carrier of siRNA. J. Cell. Biochem. 113: 619–628, 2012. © 2011 Wiley Periodicals, Inc.

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