Fecal excretion of orally administered collagen-like peptides in rats: Contribution of the triple-helical conformation to their stability

Takaki Koide, Naoyuki Yamamoto, Kazuma B. Taira, Hiroyuki Yasui

    Research output: Contribution to journalArticle

    8 Citations (Scopus)

    Abstract

    Orally ingested peptides are generally digested in the gastrointestinal (GI) tract and absorbed in the form of oligopeptides. We previously reported that intravenously administered collagen-like triple-helical peptides circulated in the bloodstream and were excreted in their intact forms in urine nearly quantitatively. In the present study, we investigated the fates of orally administered collagen-like peptides in rats. (Pro-Hyp-Gly)10 (Hyp: 4-hydroxyproline), which formed a stable triple-helical structure, was stable in the GI tract, and 72.3±13.0% of the peptide was excreted in the feces. Its recovery ratio was similar to that of all-D-(Pro-Pro-Gly)10 (75.1±15.7%), the indigestible control. In contrast, (Pro-Hyp-Gly)5 and (Pro-Pro-Gly)10, the random coil conformations of which were dominant at body temperature, were not detected in fecal samples, indicating that they were digested by proteases. The high stability of the triple-helical conformation in mammalian bodies suggests the potential use of collagen-like peptides as novel scaffolds of peptide drugs.

    Original languageEnglish
    Pages (from-to)135-137
    Number of pages3
    JournalBiological and Pharmaceutical Bulletin
    Volume39
    Issue number1
    Publication statusPublished - 2016 Jan 1

    Fingerprint

    Collagen
    Peptides
    Gastrointestinal Tract
    Oligopeptides
    Hydroxyproline
    Body Temperature
    Feces
    Peptide Hydrolases
    Urine
    Pharmaceutical Preparations
    (prolyl-prolyl-glycine)10

    Keywords

    • Collagen
    • Digestion
    • Feces
    • Peptide
    • Triple helix

    ASJC Scopus subject areas

    • Pharmaceutical Science
    • Pharmacology

    Cite this

    Fecal excretion of orally administered collagen-like peptides in rats : Contribution of the triple-helical conformation to their stability. / Koide, Takaki; Yamamoto, Naoyuki; Taira, Kazuma B.; Yasui, Hiroyuki.

    In: Biological and Pharmaceutical Bulletin, Vol. 39, No. 1, 01.01.2016, p. 135-137.

    Research output: Contribution to journalArticle

    @article{29a5cca9c61a4423a57df1c6b55bed7b,
    title = "Fecal excretion of orally administered collagen-like peptides in rats: Contribution of the triple-helical conformation to their stability",
    abstract = "Orally ingested peptides are generally digested in the gastrointestinal (GI) tract and absorbed in the form of oligopeptides. We previously reported that intravenously administered collagen-like triple-helical peptides circulated in the bloodstream and were excreted in their intact forms in urine nearly quantitatively. In the present study, we investigated the fates of orally administered collagen-like peptides in rats. (Pro-Hyp-Gly)10 (Hyp: 4-hydroxyproline), which formed a stable triple-helical structure, was stable in the GI tract, and 72.3±13.0{\%} of the peptide was excreted in the feces. Its recovery ratio was similar to that of all-D-(Pro-Pro-Gly)10 (75.1±15.7{\%}), the indigestible control. In contrast, (Pro-Hyp-Gly)5 and (Pro-Pro-Gly)10, the random coil conformations of which were dominant at body temperature, were not detected in fecal samples, indicating that they were digested by proteases. The high stability of the triple-helical conformation in mammalian bodies suggests the potential use of collagen-like peptides as novel scaffolds of peptide drugs.",
    keywords = "Collagen, Digestion, Feces, Peptide, Triple helix",
    author = "Takaki Koide and Naoyuki Yamamoto and Taira, {Kazuma B.} and Hiroyuki Yasui",
    year = "2016",
    month = "1",
    day = "1",
    language = "English",
    volume = "39",
    pages = "135--137",
    journal = "Biological and Pharmaceutical Bulletin",
    issn = "0918-6158",
    publisher = "Pharmaceutical Society of Japan",
    number = "1",

    }

    TY - JOUR

    T1 - Fecal excretion of orally administered collagen-like peptides in rats

    T2 - Contribution of the triple-helical conformation to their stability

    AU - Koide, Takaki

    AU - Yamamoto, Naoyuki

    AU - Taira, Kazuma B.

    AU - Yasui, Hiroyuki

    PY - 2016/1/1

    Y1 - 2016/1/1

    N2 - Orally ingested peptides are generally digested in the gastrointestinal (GI) tract and absorbed in the form of oligopeptides. We previously reported that intravenously administered collagen-like triple-helical peptides circulated in the bloodstream and were excreted in their intact forms in urine nearly quantitatively. In the present study, we investigated the fates of orally administered collagen-like peptides in rats. (Pro-Hyp-Gly)10 (Hyp: 4-hydroxyproline), which formed a stable triple-helical structure, was stable in the GI tract, and 72.3±13.0% of the peptide was excreted in the feces. Its recovery ratio was similar to that of all-D-(Pro-Pro-Gly)10 (75.1±15.7%), the indigestible control. In contrast, (Pro-Hyp-Gly)5 and (Pro-Pro-Gly)10, the random coil conformations of which were dominant at body temperature, were not detected in fecal samples, indicating that they were digested by proteases. The high stability of the triple-helical conformation in mammalian bodies suggests the potential use of collagen-like peptides as novel scaffolds of peptide drugs.

    AB - Orally ingested peptides are generally digested in the gastrointestinal (GI) tract and absorbed in the form of oligopeptides. We previously reported that intravenously administered collagen-like triple-helical peptides circulated in the bloodstream and were excreted in their intact forms in urine nearly quantitatively. In the present study, we investigated the fates of orally administered collagen-like peptides in rats. (Pro-Hyp-Gly)10 (Hyp: 4-hydroxyproline), which formed a stable triple-helical structure, was stable in the GI tract, and 72.3±13.0% of the peptide was excreted in the feces. Its recovery ratio was similar to that of all-D-(Pro-Pro-Gly)10 (75.1±15.7%), the indigestible control. In contrast, (Pro-Hyp-Gly)5 and (Pro-Pro-Gly)10, the random coil conformations of which were dominant at body temperature, were not detected in fecal samples, indicating that they were digested by proteases. The high stability of the triple-helical conformation in mammalian bodies suggests the potential use of collagen-like peptides as novel scaffolds of peptide drugs.

    KW - Collagen

    KW - Digestion

    KW - Feces

    KW - Peptide

    KW - Triple helix

    UR - http://www.scopus.com/inward/record.url?scp=84954436214&partnerID=8YFLogxK

    UR - http://www.scopus.com/inward/citedby.url?scp=84954436214&partnerID=8YFLogxK

    M3 - Article

    C2 - 26725436

    AN - SCOPUS:84954436214

    VL - 39

    SP - 135

    EP - 137

    JO - Biological and Pharmaceutical Bulletin

    JF - Biological and Pharmaceutical Bulletin

    SN - 0918-6158

    IS - 1

    ER -