FLAG tagging by CuAAC and nanogram-scale purification of the target protein for a bioactive metabolite involved in circadian rhythmic leaf movement in Leguminosae

Manabe, Yoshiyuki; Mukai, Makoto; Ito, Satoko; Kato, Norihiro; Ueda, Minoru

doi:10.1039/b915843j

Cited by 22 publications

(22 citation statements)

References 30 publications

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“…5a) (20). We planned to identify the target protein of 8 using the molecular probe (21). As mentioned earlier, a major problem with this approach is non-specific binding; however, we were unable to use the enantiodifferential approach because this compound and its enantiomer exhibit exactly the same bioactivity.…”

Section: Identification Of Lof Target Protein Using Click Chemistrymentioning

confidence: 99%

Chemical Biology of Glycoside-Type Bioactive Substances Controlling Nyctinastic Movement in Leguminous Plants

Manabe

Inomata

2010

TIGG

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Leguminous plants open their leaves during the day and close them at night as if sleeping, a type of movement that follows circadian rhythms and is known as nyctinastic movement. This phenomenon is controlled by two endogenous bioactive substances that exhibit opposing activities: LeafOpening Factor (LOF), which opens the leaves, and LeafClosing Factor (LCF), which closes them. The authors have carried out chemical biological research using these bioactive substances in order to clarify the mechanisms of nyctinastic movement. Here, we report on the detection and identification of the target proteins of these compounds using original methodology.

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Section: Identification Of Lof Target Protein Using Click Chemistrymentioning

confidence: 99%

Chemical Biology of Glycoside-Type Bioactive Substances Controlling Nyctinastic Movement in Leguminous Plants

Manabe

Inomata

2010

TIGG

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“…We synthesized molecular probe 14 with the tosyl group as a reacting group and azide as a pre-tag group. 15,16) An additional aromatic group was inserted in the middle of the linker part to enhance maltase inhibition by hydrophobic interaction. The intestinal glucosidase inhibitory activity of 14 was estimated to be IC 50 ¼ 22 mM against maltase and IC 50 > 100 mM (25% at 100 mM) against sucrase.…”

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confidence: 99%

“…[14][15][16] As a first set of derivatives, phenolic hydroxyl and amine group modified derivatives were synthesized and tested for their sucrase and maltase inhibitory activity to determine whether can be utilized to attach a functional group (Experimental procedures; see Biosci. Biotechnol.…”

mentioning

confidence: 99%

Synthesis and the Intestinal Glucosidase Inhibitory Activity of 2-Aminoresorcinol Derivatives toward an Investigation of Its Binding Site

Kato

Oikawa

Takahashi

et al. 2012

Bioscience, Biotechnology, and Biochemistry

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2-Aminoresorcinol is a potent and selective intestinal glucosidase inhibitor. Unlike the majority of glucosidase inhibitors, it shows an uncompetitive mode of inhibition. In this study, we tested the intestinal glucosidase inhibitory activity of various 2-aminoresorcinol derivatives. We found that structural changes, in amino and two phenolic hydroxyl groups had a negative impact on inhibitory activity, but methylation of the phenolic hydroxyl group was found to maintain its activity and replacement of the aromatic ring with an acyl or alkoxy carbonyl group at the 4th position also retained its activity. This enable us to design a molecular probe for further study of the inhibition mechanism of 2-aminoresorcinol.

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“…was used for CuAAC coupling with fluorescein isothiocyanate (FITC)-alkyne (16) 16) to give FITC-labeled COR (17) in almost quantitative yield (Scheme 1). Further bioorganic studies using 17 will be reported in elsewhere.…”

Section: à9mentioning

confidence: 99%

Azido-Coronatine: A Useful Platform for “Click Chemistry”-Mediated Probe Synthesis for Bioorganic Studies

Okada

Egoshi

2010

Bioscience, Biotechnology, and Biochemistry

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We report on the development of azide-coronatine as a useful platform for azide alkyne cycloaddition (''click chemistry'')-mediated synthesis of molecular probes. (þ)-Azido-coronatine was synthesized in 10 steps with 11% yield using improved synthesis of coronafacic acid, in which the highly exo-selective Diels-Alder reaction (endo:exo > 1:25) is the key step. Azido coronatine was as effective as the original coronatine in a stomatal opening assay, and was easily modified to a fluorescein isothiocyanate (FITC)-labeled probe with high yield.

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FLAG tagging by CuAAC and nanogram-scale purification of the target protein for a bioactive metabolite involved in circadian rhythmic leaf movement in Leguminosae

Cited by 22 publications

References 30 publications

Chemical Biology of Glycoside-Type Bioactive Substances Controlling Nyctinastic Movement in Leguminous Plants

Chemical Biology of Glycoside-Type Bioactive Substances Controlling Nyctinastic Movement in Leguminous Plants

Synthesis and the Intestinal Glucosidase Inhibitory Activity of 2-Aminoresorcinol Derivatives toward an Investigation of Its Binding Site

Azido-Coronatine: A Useful Platform for “Click Chemistry”-Mediated Probe Synthesis for Bioorganic Studies

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