Cellular uptake of IgG using collagen-like cell-penetrating peptides

Ryo Masuda, Kazuhiro Yamamoto, Takaki Koide

    Research output: Contribution to journalArticle

    4 Citations (Scopus)

    Abstract

    Cell-penetrating peptides (CPPs) are attractive tools for delivering macromolecules that have poor membrane permeability, such as antibodies, into cells. However, the major drawback of conventional CPPs is their instability in bodily fluids. We previously reported a novel CPP employing a collagen-like triple-helical structure that exhibited remarkable resistance against serum proteases. Herein, we report the delivery of full-length immunoglobulin G (IgG) antibody into cells using a triple-helical CPP. The CPP was conjugated to IgG via a one-pot reaction using 2-iminothiolane as a crosslinking reagent. The triple-helical CPP was less prone to being aggregated and neutralized by serum than was octaarginine, a conventional CPP. However, most of the conjugates were found to be entrapped in endosomes.

    Original languageEnglish
    Pages (from-to)130-134
    Number of pages5
    JournalBiological and Pharmaceutical Bulletin
    Volume39
    Issue number1
    Publication statusPublished - 2016 Jan 1

    Fingerprint

    Cell-Penetrating Peptides
    Collagen
    Immunoglobulin G
    Cross-Linking Reagents
    Antibodies
    Endosomes
    Serum
    Permeability
    Peptide Hydrolases
    Membranes

    Keywords

    • Antibody delivery
    • Cell-penetrating peptide
    • Collagen-like peptide
    • Peptide conjugation

    ASJC Scopus subject areas

    • Pharmaceutical Science
    • Pharmacology

    Cite this

    Cellular uptake of IgG using collagen-like cell-penetrating peptides. / Masuda, Ryo; Yamamoto, Kazuhiro; Koide, Takaki.

    In: Biological and Pharmaceutical Bulletin, Vol. 39, No. 1, 01.01.2016, p. 130-134.

    Research output: Contribution to journalArticle

    @article{6a16398921aa474cb848dd8faf1b7eb3,
    title = "Cellular uptake of IgG using collagen-like cell-penetrating peptides",
    abstract = "Cell-penetrating peptides (CPPs) are attractive tools for delivering macromolecules that have poor membrane permeability, such as antibodies, into cells. However, the major drawback of conventional CPPs is their instability in bodily fluids. We previously reported a novel CPP employing a collagen-like triple-helical structure that exhibited remarkable resistance against serum proteases. Herein, we report the delivery of full-length immunoglobulin G (IgG) antibody into cells using a triple-helical CPP. The CPP was conjugated to IgG via a one-pot reaction using 2-iminothiolane as a crosslinking reagent. The triple-helical CPP was less prone to being aggregated and neutralized by serum than was octaarginine, a conventional CPP. However, most of the conjugates were found to be entrapped in endosomes.",
    keywords = "Antibody delivery, Cell-penetrating peptide, Collagen-like peptide, Peptide conjugation",
    author = "Ryo Masuda and Kazuhiro Yamamoto and Takaki Koide",
    year = "2016",
    month = "1",
    day = "1",
    language = "English",
    volume = "39",
    pages = "130--134",
    journal = "Biological and Pharmaceutical Bulletin",
    issn = "0918-6158",
    publisher = "Pharmaceutical Society of Japan",
    number = "1",

    }

    TY - JOUR

    T1 - Cellular uptake of IgG using collagen-like cell-penetrating peptides

    AU - Masuda, Ryo

    AU - Yamamoto, Kazuhiro

    AU - Koide, Takaki

    PY - 2016/1/1

    Y1 - 2016/1/1

    N2 - Cell-penetrating peptides (CPPs) are attractive tools for delivering macromolecules that have poor membrane permeability, such as antibodies, into cells. However, the major drawback of conventional CPPs is their instability in bodily fluids. We previously reported a novel CPP employing a collagen-like triple-helical structure that exhibited remarkable resistance against serum proteases. Herein, we report the delivery of full-length immunoglobulin G (IgG) antibody into cells using a triple-helical CPP. The CPP was conjugated to IgG via a one-pot reaction using 2-iminothiolane as a crosslinking reagent. The triple-helical CPP was less prone to being aggregated and neutralized by serum than was octaarginine, a conventional CPP. However, most of the conjugates were found to be entrapped in endosomes.

    AB - Cell-penetrating peptides (CPPs) are attractive tools for delivering macromolecules that have poor membrane permeability, such as antibodies, into cells. However, the major drawback of conventional CPPs is their instability in bodily fluids. We previously reported a novel CPP employing a collagen-like triple-helical structure that exhibited remarkable resistance against serum proteases. Herein, we report the delivery of full-length immunoglobulin G (IgG) antibody into cells using a triple-helical CPP. The CPP was conjugated to IgG via a one-pot reaction using 2-iminothiolane as a crosslinking reagent. The triple-helical CPP was less prone to being aggregated and neutralized by serum than was octaarginine, a conventional CPP. However, most of the conjugates were found to be entrapped in endosomes.

    KW - Antibody delivery

    KW - Cell-penetrating peptide

    KW - Collagen-like peptide

    KW - Peptide conjugation

    UR - http://www.scopus.com/inward/record.url?scp=84954491764&partnerID=8YFLogxK

    UR - http://www.scopus.com/inward/citedby.url?scp=84954491764&partnerID=8YFLogxK

    M3 - Article

    C2 - 26725435

    AN - SCOPUS:84954491764

    VL - 39

    SP - 130

    EP - 134

    JO - Biological and Pharmaceutical Bulletin

    JF - Biological and Pharmaceutical Bulletin

    SN - 0918-6158

    IS - 1

    ER -