A Self-Assembled Spherical Complex Displaying a Gangliosidic Glycan Cluster Capable of Interacting with Amyloidogenic Proteins

Sota Sato, Yutaka Yoshimasa, Daishi Fujita, Maho Yagi-Utsumi, Takumi Yamaguchi, Koichi Kato, Makoto Fujita

    Research output: Contribution to journalArticlepeer-review

    26 Citations (Scopus)

    Abstract

    Physiological and pathological functions of glycans are promoted through their clustering effects as exemplified by a series of gangliosides, sialylated glycosphingolipids, which serve as acceptors for bacterial toxins and viruses. Furthermore, ganglioside GM1 clusters on neuronal cell membranes specifically interact with amyloidogenic proteins, triggering their conformational transitions and leading to neurodegeneration. Here we develop a self-assembled spherical complex that displays a cluster of the GM1 pentasaccharide, and successfully demonstrate its ability to interact with amyloid β and α-synuclein. Due to the lack of hydrophobic lipid moieties, which would stably trap these cohesive proteins or give rise to toxic aggregates, this artificial cluster enabled NMR spectroscopic characterization of the early encounter stage of protein interactions with its outer carbohydrate moieties, which were not observable with previous glycan clusters.

    Original languageEnglish
    Pages (from-to)8435-8439
    Number of pages5
    JournalAngewandte Chemie - International Edition
    Volume54
    Issue number29
    DOIs
    Publication statusPublished - 2015 Jul 13

    Keywords

    • NMR spectroscopy
    • amyloid β
    • self-assembly
    • sugar cluster
    • α-synuclein

    ASJC Scopus subject areas

    • Catalysis
    • Chemistry(all)

    Fingerprint Dive into the research topics of 'A Self-Assembled Spherical Complex Displaying a Gangliosidic Glycan Cluster Capable of Interacting with Amyloidogenic Proteins'. Together they form a unique fingerprint.

    Cite this