Synthesis of the enantiomers of XYLNAc and LYXNAc: Comparison of β-N-acetylhexosaminidase inhibition by the 8 stereoisomers of 2-N-acetylamino-1,2,4-trideoxy-1,4-iminopentitols

Elizabeth V. Crabtree; R. Fernando Martínez; Shinpei Nakagawa; Isao Adachi; Terry D. Butters; Atsushi Kato; George W.J. Fleet; Andreas F.G. Glawar

doi:10.1039/c4ob00097h

Synthesis of the enantiomers of XYLNAc and LYXNAc: Comparison of β-N-acetylhexosaminidase inhibition by the 8 stereoisomers of 2-N-acetylamino-1,2,4-trideoxy-1,4-iminopentitols

Elizabeth V. Crabtree, R. Fernando Martínez, Shinpei Nakagawa, Isao Adachi, Terry D. Butters, Atsushi Kato^*, George W.J. Fleet, Andreas F.G. Glawar

^*この論文の責任著者

薬剤部

研究成果: ジャーナルへの寄稿 › 学術論文 › 査読

19 被引用数 (Scopus)

抄録

The enantiomers of XYLNAc (2-N-acetylamino-1,2,4-trideoxy-1,4-iminoxylitol) are prepared from the enantiomers of glucuronolactone; the synthesis of the enantiomers of LYXNAc (2-N-acetylamino-1,2,4-trideoxy-1,4-iminolyxitol) from an l-arabinono-δ-lactone and a d-ribono-δ-lactone is reported. A comparison is made of the inhibition of β-N-acetylhexosaminidases (HexNAcases) and α-N-acetylgalactosaminidase (α-GalNAcase) by 8 stereoisomeric 2-N-acetylamino-1,2,4-trideoxy-1,4-iminopentitols; their N-benzyl derivatives are better inhibitors than the parent compounds. Both XYLNAc and LABNAc are potent inhibitors against HexNAcases. None of the compounds show any inhibition of α-GalNAcase. This journal is

本文言語	英語
ページ（範囲）	3932-3943
ページ数	12
ジャーナル	Organic and Biomolecular Chemistry
巻	12
号	23
DOI	https://doi.org/10.1039/c4ob00097h
出版ステータス	出版済み - 2014/06/21

ASJC Scopus 主題領域

生化学
物理化学および理論化学
有機化学

文献へのアクセス

10.1039/c4ob00097h

フィンガープリント

「Synthesis of the enantiomers of XYLNAc and LYXNAc: Comparison of β-N-acetylhexosaminidase inhibition by the 8 stereoisomers of 2-N-acetylamino-1,2,4-trideoxy-1,4-iminopentitols」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。

引用スタイル

Crabtree, E. V., Martínez, R. F., Nakagawa, S., Adachi, I., Butters, T. D., Kato, A., Fleet, G. W. J., & Glawar, A. F. G. (2014). Synthesis of the enantiomers of XYLNAc and LYXNAc: Comparison of β-N-acetylhexosaminidase inhibition by the 8 stereoisomers of 2-N-acetylamino-1,2,4-trideoxy-1,4-iminopentitols. Organic and Biomolecular Chemistry, 12(23), 3932-3943. https://doi.org/10.1039/c4ob00097h

@article{98aac4bd0f5e4c15b70e84a8ef475a20,

title = "Synthesis of the enantiomers of XYLNAc and LYXNAc: Comparison of β-N-acetylhexosaminidase inhibition by the 8 stereoisomers of 2-N-acetylamino-1,2,4-trideoxy-1,4-iminopentitols",

abstract = "The enantiomers of XYLNAc (2-N-acetylamino-1,2,4-trideoxy-1,4-iminoxylitol) are prepared from the enantiomers of glucuronolactone; the synthesis of the enantiomers of LYXNAc (2-N-acetylamino-1,2,4-trideoxy-1,4-iminolyxitol) from an l-arabinono-δ-lactone and a d-ribono-δ-lactone is reported. A comparison is made of the inhibition of β-N-acetylhexosaminidases (HexNAcases) and α-N-acetylgalactosaminidase (α-GalNAcase) by 8 stereoisomeric 2-N-acetylamino-1,2,4-trideoxy-1,4-iminopentitols; their N-benzyl derivatives are better inhibitors than the parent compounds. Both XYLNAc and LABNAc are potent inhibitors against HexNAcases. None of the compounds show any inhibition of α-GalNAcase. This journal is",

author = "Crabtree, {Elizabeth V.} and Mart{\'i}nez, {R. Fernando} and Shinpei Nakagawa and Isao Adachi and Butters, {Terry D.} and Atsushi Kato and Fleet, {George W.J.} and Glawar, {Andreas F.G.}",

year = "2014",

month = jun,

day = "21",

doi = "10.1039/c4ob00097h",

language = "英語",

volume = "12",

pages = "3932--3943",

journal = "Organic and Biomolecular Chemistry",

issn = "1477-0520",

publisher = "Royal Society of Chemistry",

number = "23",

}

Crabtree, EV, Martínez, RF, Nakagawa, S, Adachi, I, Butters, TD, Kato, A, Fleet, GWJ & Glawar, AFG 2014, 'Synthesis of the enantiomers of XYLNAc and LYXNAc: Comparison of β-N-acetylhexosaminidase inhibition by the 8 stereoisomers of 2-N-acetylamino-1,2,4-trideoxy-1,4-iminopentitols', Organic and Biomolecular Chemistry, vol. 12, no. 23, pp. 3932-3943. https://doi.org/10.1039/c4ob00097h

Synthesis of the enantiomers of XYLNAc and LYXNAc: Comparison of β-N-acetylhexosaminidase inhibition by the 8 stereoisomers of 2-N-acetylamino-1,2,4-trideoxy-1,4-iminopentitols. / Crabtree, Elizabeth V.; Martínez, R. Fernando; Nakagawa, Shinpei その他.
In: Organic and Biomolecular Chemistry, Vol. 12, No. 23, 21.06.2014, p. 3932-3943.

研究成果: ジャーナルへの寄稿 › 学術論文 › 査読

TY - JOUR

T1 - Synthesis of the enantiomers of XYLNAc and LYXNAc

T2 - Comparison of β-N-acetylhexosaminidase inhibition by the 8 stereoisomers of 2-N-acetylamino-1,2,4-trideoxy-1,4-iminopentitols

AU - Crabtree, Elizabeth V.

AU - Martínez, R. Fernando

AU - Nakagawa, Shinpei

AU - Adachi, Isao

AU - Butters, Terry D.

AU - Kato, Atsushi

AU - Fleet, George W.J.

AU - Glawar, Andreas F.G.

PY - 2014/6/21

Y1 - 2014/6/21

N2 - The enantiomers of XYLNAc (2-N-acetylamino-1,2,4-trideoxy-1,4-iminoxylitol) are prepared from the enantiomers of glucuronolactone; the synthesis of the enantiomers of LYXNAc (2-N-acetylamino-1,2,4-trideoxy-1,4-iminolyxitol) from an l-arabinono-δ-lactone and a d-ribono-δ-lactone is reported. A comparison is made of the inhibition of β-N-acetylhexosaminidases (HexNAcases) and α-N-acetylgalactosaminidase (α-GalNAcase) by 8 stereoisomeric 2-N-acetylamino-1,2,4-trideoxy-1,4-iminopentitols; their N-benzyl derivatives are better inhibitors than the parent compounds. Both XYLNAc and LABNAc are potent inhibitors against HexNAcases. None of the compounds show any inhibition of α-GalNAcase. This journal is

AB - The enantiomers of XYLNAc (2-N-acetylamino-1,2,4-trideoxy-1,4-iminoxylitol) are prepared from the enantiomers of glucuronolactone; the synthesis of the enantiomers of LYXNAc (2-N-acetylamino-1,2,4-trideoxy-1,4-iminolyxitol) from an l-arabinono-δ-lactone and a d-ribono-δ-lactone is reported. A comparison is made of the inhibition of β-N-acetylhexosaminidases (HexNAcases) and α-N-acetylgalactosaminidase (α-GalNAcase) by 8 stereoisomeric 2-N-acetylamino-1,2,4-trideoxy-1,4-iminopentitols; their N-benzyl derivatives are better inhibitors than the parent compounds. Both XYLNAc and LABNAc are potent inhibitors against HexNAcases. None of the compounds show any inhibition of α-GalNAcase. This journal is

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U2 - 10.1039/c4ob00097h

DO - 10.1039/c4ob00097h

M3 - 学術論文

C2 - 24802185

AN - SCOPUS:84901251361

SN - 1477-0520

VL - 12

SP - 3932

EP - 3943

JO - Organic and Biomolecular Chemistry

JF - Organic and Biomolecular Chemistry

IS - 23

ER -