Papers - Sato, Toshinori

Izenamides A and B, Statine-Containing Depsipeptides, and an Analogue from a Marine Cyanobacterium

Kanamori Y., Iwasaki A., Sumimoto S., Matsubara T., Sato T., Suenaga K.

Journal of Natural Products (Journal of Natural Products)  81 ( 7 ) 1673 - 1681 2018.07

ISSN  01633864

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© 2018 American Chemical Society and American Society of Pharmacognosy. Izenamides A, B, and C (1-3), new linear depsipeptides, were isolated from a taxonomically distinct marine cyanobacterium. Izenamides A and B contain a statine moiety [(3S,4S)-4-amino-3-hydroxy-6-methylheptanoic acid] and inhibited the activity of cathepsin D, an aspartic peptidase. Meanwhile, izenamides did not show growth-inhibitory activity against HeLa, HL60, or MCF-7 cells at up to 10 μM.

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Comparative Quantification Method for Glycosylated Products Elongated on β-Xylosides Using a Stable Isotope-Labeled Saccharide Primer

Otsuka Y., Sato T.

Analytical Chemistry (Analytical Chemistry)  90 ( 8 ) 5201 - 5208 2018.04

ISSN  00032700

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© 2018 American Chemical Society. The structures and amounts of glycosaminoglycan (GAG) produced by cells have attracted much interest because GAG biosynthesis activity can change in cellular processes such as disease and differentiation. β-Xylosides, also called saccharide primers, have been used as artificial acceptors not only to generate GAG oligosaccharides in cells and tissues but also to investigate their biosynthetic pathways. Various analytical methods have been applied to confirm the structure and amounts of GAG oligosaccharides elongated using saccharide primers, yet sample preparation processes such as solid-phase extraction in analysis can cause experimental error and disrupt accurate comparative quantification of glycosylated products. In this study, we developed a new quantification method using a deuterium-labeled saccharide primer. The "heavy" and "light" primers were chemically synthesized, and priming abilities were confirmed by liquid chromatography-tandem mass spectrometry. Relative peak areas of light/heavy products showed good linearity and were well correlated with the theoretical amounts of glycosylated products. Then, as a validation study, we carried out a biosynthesis inhibition assay using known GAG biosynthesis inhibitors. According to the relative quantification using saccharide primers, differences in the mode-of-action among the four GAG biosynthesis inhibitors were dependent on the GAG biosynthetic pathway. Our results indicate that the method will likely forge a new path for comparative glycosaminoglycomics using cultured cells and tissues.

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Novel hemagglutinin-binding sulfated oligofucosides and their effect on influenza virus infection

Kosono S., Kasai A., Komaba S., Matsubara T., Sato T., Takahashi D., Toshima K.

Chemical Communications (Chemical Communications)  54 ( 54 ) 7467 - 7470 2018

ISSN  13597345

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© 2018 The Royal Society of Chemistry. Among a series of chemically synthesized fucoidan derivatives (1-9), 5 was found for the first time to bind to influenza virus hemagglutinins (HAs) and inhibit hemagglutination activity. In addition, a designed C3-symmetric tripodal ligand 10, synthesized with three sulfated oligofucoside moieties of 5, exhibited much greater hemagglutination inhibition activity than 5. A plaque assay using MDCK cells demonstrated that 10 effectively inhibited influenza virus infection.

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Glycoreplica peptides

Matsubara T., Sato T., Taki T.

Methods in Molecular Biology (Methods in Molecular Biology)  1804   437 - 447 2018

ISSN  10643745

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© 2018, Springer Science+Business Media, LLC, part of Springer Nature. “Glycoreplica peptides” are prepared using a phage display peptide library and monoclonal antibodies that recognize the carbohydrate epitopes of glycoconjugate antigens. The peptides obtained not only mimic the shapes of original glycoconjugate antigens but also have some of their functions. We herein describe how to identify the amino acid alignments of glycoreplica peptides using phage display selection against carbohydrate-binding proteins. Target-specific peptides and proteins may be selected from the large repertory of a peptide/protein library using phage display technology. Glycoreplica peptides have the potential to become alternatives to carbohydrate ligands such as mimotopes for vaccinations and carbohydrate-derived drugs for carbohydrate-related diseases.

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Amyloid- fibrils assembled on ganglioside-enriched membranes contain both parallel -sheets and turns

Matsubara T., Yasumori H., Ito K., Shimoaka T., Hasegawa T., Sato T.

Journal of Biological Chemistry (Journal of Biological Chemistry)  293 ( 36 ) 14146 - 14154 2018

ISSN  00219258

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© 2018 Matsubara et al. Some protein and peptide aggregates, such as those of amyloid- protein (A), are neurotoxic and have been implicated in several neurodegenerative diseases. A accumulates at nanoclusters enriched in neuronal lipids called gangliosides in the presynaptic neuronal membrane, and the resulting oligomeric and/or fibrous forms accelerate the development of Alzheimer’s disease. Although the presence of A deposits at such nanoclusters is known, the mechanism of their assembly and the relationship between A secondary structure and topography are still unclear. Here, we first confirmed by atomic force microscopy that A 40 fibrils can be obtained by incubating seed-free A 40 monomers with a membrane composed of sphingomyelin, cholesterol, and the ganglioside GM1. Using Fourier transform infrared (FTIR) reflection–absorption spectroscopy, we then found that these lipid-associated fibrils contained parallel -sheets, whereas self-assembled A 40 molecules formed antiparallel -sheets. We also found that the fibrils obtained at GM1-rich nanoclusters were generated from turn A 40 . Our findings indicate that A generally self-assembles into antiparallel -structures but can also form protofibrils with parallel -sheets by interacting with ganglioside-bound A. We concluded that by promoting the formation of parallel -sheets, highly ganglioside-enriched nanoclusters help accelerate the elongation of A fibrils. These results advance our understanding of ganglioside-induced A fibril formation in neuronal membranes and may help inform the development of additional therapies for Alzheimer’s disease.

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Size and shape of amyloid fibrils induced by ganglioside nanoclusters: role of sialyl oligosaccharide in fibril formation

Teruhiko Matsubara, Masaya Nishihara, Hanaki Yasumori, Mako Nakai, Katsuhiko Yanagisawa, Toshinori Sato

Langmuir 33   13874 - 13881 2017

Research paper (scientific journal), Joint Work, Accepted

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Selective intracellular delivery of ganglioside GM3-binding peptide through caveolae/raft-mediated endocytosis

SATO TOSHINORI

Biomacromolecules, 18   355 - 362 2017

Research paper (scientific journal), Joint Work, Accepted

Saccharide primers comprising xylosyl-serine primed phosphorylated oligosaccharides act as intermediates in glycosaminoglycan biosynthesis

Yuya Otsuka, Toshinori Sato

ACS Omega 2   3110 - 3122 2017

Research paper (scientific journal), Joint Work, Accepted

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Kohamamides A, B and C, Cyclic Depsipeptides from an Okeania sp. Marine Cyanobacterium

Arihiro Iwasaki, Ikuma Shiota, Shimpei Sumimoto, Teruhiko Matsubara, Toshinori Sato, Kiyotake Suenaga

J. Nat. Prod. 80   1948 - 1952 2017

Research paper (scientific journal), Accepted

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In vitro and in vivo gene delivery using chitosan/hyaluronic acid nanoparticles: Influences of molecular mass of hyaluronic acid and lyophilization on the transfection efficiency

Toshinori Sato, Mitsuhiro Nakata, Zhihong Yang, Yu Torizuka, Satoko Kishimoto, Masayuki Ishihara

J. Gene Med. 19   e2968 2017

Research paper (scientific journal), Joint Work, Accepted

Design of glycopolymers carrying sialyl oligosaccharides for controlling the interaction with the influenza virus

Masanori Nagao, Yurina Fujiwara, Teruhiko Matsubara, Yu Hoshino, Toshinori Sato, Yoshiko Miura

Biomacromolecules 18   4385 - 4392 2017

Research paper (scientific journal), Joint Work, Accepted

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Highly sensitive detection of influenza virus by boron-doped diamond electrode terminated with sialic acid-mimic peptide

SATO TOSHINORI

Proc. Natl. Acad. Sci. USA 113 ( 32 ) 8981 - 8984 2016

Research paper (scientific journal), Joint Work, Accepted

Functional Domains of ZFP809 Essential for Nuclear Localization and Gene Silencing,

Yu Ichida, Yuko Utsunomiya Y, Junko Tomikawa, Kazuhiko Nakabayashi, Toshinori Sato, Masafumi Onodera

Biosci. Biotech. Biochem. 80   114 - 120 2016

Research paper (scientific journal), Joint Work, Accepted

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体液類似環境におけるアパタイト結合性ペプチド樹状オリゴマーによるミネラリゼーション

橋詰　峰雄、小野上　綾乃、飯島　一智、松原　輝彦、内田　祐樹、佐藤　智典

高分子論文集 73   55 - 61 2016

Research paper (scientific journal), Accepted

糖鎖模倣ペプチドのインフルエンザヘマグルチニンに対する結合活性の多価効果

松原 輝彦、大西 愛、齋藤 智美、山口 大介、佐藤 智典

高分子論文集 73   62 - 68 2016

Research paper (scientific journal), Joint Work, Accepted

Heptapeptide Ligands against Receptor-Binding Sites of Influenza Hemagglutinin toward Anti-Influenza Therapy

Teruhiko Matsubara, Ai Onishi, Daisuke Yamaguchi, Toshinori Sato

Bioorg. Med. Chem. 24   1106 - 1114 2016

Research paper (scientific journal), Accepted

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Binding of Hemagglutinin and Influenza Virus to a Peptide-Conjugated Lipid Membrane

Teruhiko Matsubara, Rabi Shibata, Toshinori Sato

Front. Microbiol. 7   468 2016

Research paper (scientific journal), Joint Work, Accepted

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Imbalance in fatty-acid-chain length of gangliosides triggers Alzheimer amyloid deposition in the precuneus, Naoto Oikawa

Teruhiko Matsubara, Ryoto Fukuda, Hanaki Yasumori, Hiroyuki Hatsuta, Shigeo Murayama, Toshinori Sato, Akemi Suzuki, Katsuhiko Yanagisawa

PLOS ONE 10 ( 3 ) e0121356 2015

Research paper (scientific journal), Joint Work, Accepted

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Mebamamides A and B, Cyclic Lipopeptides Isolated from the Green Alga Derbesia marina

Arihiro Iwasaki, Osamu Ohno, Shinpei Sumimoto, Teruhiko Matsubara, Satoshi Shimada, Toshinori Sato, and Kiyotake Suenaga

J. Nat. Prod. ７８   901 - 908 2015

Research paper (scientific journal)

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Glycolipid dynamics in generation and differentiation of induced pluripotent stem cells

Takuma Ojima, Eri Shibata, Shiho Saito, Masashi Toyoda, Hideki Nakajima, Mayu Yamazaki-Inoue, Yoshitaka Miyagawa, Nobutaka Kiyokawa, Jun-ichiro Fujimoto, Toshinori Sato, and Akihiro Umezawa

Scientific Reports 5   14988 2015

Research paper (scientific journal), Accepted

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