Discovery of cryoprotective activity in human genome-derived intrinsically disordered proteins

Naoki Matsuo, Natsuko Goda, Kana Shimizu, Satoshi Fukuchi, Motonori Ota, Hidekazu Hiroaki

    Research output: Contribution to journalArticle

    1 Citation (Scopus)

    Abstract

    Intrinsically disordered proteins (IDPs) are an emerging phenomenon. They may have a high degree of flexibility in their polypeptide chains, which lack a stable 3D structure. Although several biological functions of IDPs have been proposed, their general function is not known. The only finding related to their function is the genetically conserved YSK2 motif present in plant dehydrins. These proteins were shown to be IDPs with the YSK2 motif serving as a core region for the dehydrins’ cryoprotective activity. Here we examined the cryoprotective activity of randomly selected IDPs toward the model enzyme lactate dehydrogenase (LDH). All five IDPs that were examined were in the range of 35–45 amino acid residues in length and were equally potent at a concentration of 50 µg/mL, whereas folded proteins, the PSD-95/Dlg/ZO-1 (PDZ) domain, and lysozymes had no potency. We further examined their cryoprotective activity toward glutathione S-transferase as an example of the other enzyme, and toward enhanced green fluorescent protein as a non-enzyme protein example. We further examined the lyophilization protective activity of the peptides toward LDH, which revealed that some IDPs showed a higher activity than that of bovine serum albumin (BSA). Based on these observations, we propose that cryoprotection is a general feature of IDPs. Our findings may become a clue to various industrial applications of IDPs in the future.

    Original languageEnglish
    Article number401
    JournalInternational Journal of Molecular Sciences
    Volume19
    Issue number2
    DOIs
    Publication statusPublished - 2018 Feb 1

    Fingerprint

    Intrinsically Disordered Proteins
    genome
    Human Genome
    Genes
    proteins
    Proteins
    L-Lactate Dehydrogenase
    lactates
    dehydrogenases
    Enzymes
    Peptides
    Freeze Drying
    enzymes
    Muramidase
    Bovine Serum Albumin
    Glutathione Transferase
    colloiding
    Industrial applications
    glutathione
    Polypeptides

    Keywords

    • Biomedical application
    • Cryoprotection
    • Dehydrin
    • Intrinsically disordered proteins
    • Lyophilization protection
    • Molecular shields

    ASJC Scopus subject areas

    • Catalysis
    • Molecular Biology
    • Spectroscopy
    • Computer Science Applications
    • Physical and Theoretical Chemistry
    • Organic Chemistry
    • Inorganic Chemistry

    Cite this

    Discovery of cryoprotective activity in human genome-derived intrinsically disordered proteins. / Matsuo, Naoki; Goda, Natsuko; Shimizu, Kana; Fukuchi, Satoshi; Ota, Motonori; Hiroaki, Hidekazu.

    In: International Journal of Molecular Sciences, Vol. 19, No. 2, 401, 01.02.2018.

    Research output: Contribution to journalArticle

    Matsuo, Naoki ; Goda, Natsuko ; Shimizu, Kana ; Fukuchi, Satoshi ; Ota, Motonori ; Hiroaki, Hidekazu. / Discovery of cryoprotective activity in human genome-derived intrinsically disordered proteins. In: International Journal of Molecular Sciences. 2018 ; Vol. 19, No. 2.
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